WO2026039627A1

WO2026039627A1 - Antibody conjugates and methods of making and using the same

Info

Publication number: WO2026039627A1
Application number: PCT/US2025/041988
Authority: WO
Inventors: Penelope DRAKE; Dharmaraj SAMUEL
Original assignee: RP Scherer Technologies LLC
Current assignee: RP Scherer Technologies LLC
Priority date: 2024-08-16
Filing date: 2025-08-14
Publication date: 2026-02-19
Anticipated expiration: 2027-02-16

Abstract

Disclosed herein are antibodies that include one or more sulfatase motifs in a constant region of an immunoglobulin (Ig) heavy chain and, optionally, an Ig light chain having a sulfatase motif in a constant region. The sulfatase motifs can be converted by a formylglycine-generating enzyme (FGE) to produce a formylglycine (fGly)-modified antibody. An fGly-modified antibody can be covalently and site-specifically bound to a moiety of interest to provide an antibody conjugate. The disclosure also encompasses methods of producing such tagged antibodies, fGly-modified antibodies, and antibody conjugates, as well as methods of using the same.

Description

Atty. Dkt: RDWD-048WO ANTIBODY CONJUGATES AND METHODS OF MAKING AND USING THE SAME CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims the benefit of priority to U.S. Provisional Application No. 63/684,168, filed August 16, 2024, the disclosure of which is incorporated herein by reference in its entirety. INCORPORATION-BY-REFERENCE OF MATERIAL ELECTRONICALLY SUBMITTED [0002] A Sequence Listing is provided herewith as a Sequence Listing XML, “RDWD- 048WO_SEQ_LIST” created on August 16, 2024 and having a size of 311,567 bytes. The contents of the Sequence Listing XML are incorporated by reference herein in their entirety. INTRODUCTION [0003] Antibody-drug conjugates (ADCs) are complex molecules comprising an antibody and a payload. Various factors affect an ADC’s biophysical and functional properties, which include clearance/exposure, efficacy, and tolerability. These functional properties are affected by factors such as the conjugation chemistry employed to attach the linker to the protein, the location of the linker attachment site on the antibody, the number of payload drugs attached per antibody, i.e., the drug-to-antibody ratio, or DAR, and other linker elements, such as cleavable and self-immolating motifs or hydrophilic elements. [0004] These same factors can also affect ADC stability, including melting temperature or thermal stability and purity including % monomeric species, conjugatability, and product yields. These aspects impact ADC manufacturability and cost of production. [0005] By 2024, twelve ADCs had been approved by the FDA for treatment of various cancers. Many more ADCs are in preclinical development or being tested in clinical studies. As ADCs become more commonly available as treatment options for patients, cost considerations will be increasingly used as decision points both in ADC discovery – by drug developers looking to reduce the cost of goods – and in the marketplace – by patients and their doctors navigating expenses as an aspect of their health care. The two major drivers of ADC manufacturing costs are antibody production and linker-payload production. Thus, the development of improved Atty. Dkt: RDWD-048WO ADCs can directly improve yields and reduce manufacturing costs. With manufacturability as a driver in both drug development and in the potential market share of an approved product, innovations that improve upon manufacturability and product yields and quality will be ever more valuable. SUMMARY [0006] In certain aspects, the disclosure provides antibodies and ADCs having improved production outcomes and that enable the production of unanticipated and unexpected molecular compositions with novel functionalities. [0007] In certain aspects, the disclosure provides antibody comprising an immunoglobulin (Ig) heavy chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence and the second amino acid sequence are selected from: SEQ ID NOs: 1 to 15. [0008] In certain embodiments, the first amino acid sequence and the second amino acid second sequence, respectively, comprise: SEQ ID NO: 6 and SEQ ID NO: 11; SEQ ID NO:15 and SEQ ID NO: 11; SEQ ID NO: 15 and SEQ ID NO: 1; SEQ ID NO: 9 and SEQ ID NO: 11; SEQ ID NO: 15 and SEQ ID NO: 9; SEQ ID NO: 15 and SEQ ID NO: 6; SEQ ID NO: 8 and SEQ ID NO: 11; SEQ ID NO: 8 and SEQ ID NO: 15; SEQ ID NO: 3 and SEQ ID NO: 11; SEQ ID NO: 3 and SEQ ID NO: 6; SEQ ID NO: 15 and SEQ ID NO: 5; SEQ ID NO: 5 and SEQ ID NO: 11; SEQ ID NO: 5 and SEQ ID NO: 9; or SEQ ID NO: 12 and SEQ ID NO: 11. Atty. Dkt: RDWD-048WO [0009] In some aspects, the disclosure provides antibodies comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, and wherein the first amino acid sequence is selected from SEQ ID NOs: 1 to 15 and the second amino acid sequence is selected from SEQ ID NOs: 16 to 20. [0010] In some cases, the first amino acid sequence and the second amino acid sequence, respectively, comprise: SEQ ID NO: 7 and SEQ ID NO: 18; SEQ ID NO: 12 and SEQ ID NO: 18; SEQ ID NO: 8 and SEQ ID NO: 18; SEQ ID NO: 11 and SEQ ID NO: 18; SEQ ID NO: 15 and SEQ ID NO: 19; SEQ ID NO: 10 and SEQ ID NO: 18; SEQ ID NO: 1 and SEQ ID NO: 18; SEQ ID NO: 5 and SEQ ID NO: 18; SEQ ID NO: 4 and SEQ ID NO: 18; SEQ ID NO: 1 and SEQ ID NO: 19; SEQ ID NO: 11 and SEQ ID NO: 19; SEQ ID NO: 5 and SEQ ID NO: 19; SEQ ID NO: 9 and SEQ ID NO: 18; SEQ ID NO: 8 and SEQ ID NO: 19; SEQ ID NO: 15 and SEQ ID NO: 18; SEQ ID NO: 6 and SEQ ID NO: 18; SEQ ID NO: 6 and SEQ ID NO: 19; SEQ ID NO: 2 and SEQ ID NO: 18; SEQ ID NO: 12 and SEQ ID NO: 19; SEQ ID NO: 4 and SEQ ID NO: 19; SEQ ID NO: 7 and SEQ ID NO: 19; SEQ ID NO: 10 and SEQ ID NO: 19; SEQ ID NO: 4 and SEQ ID NO: 20; Atty. Dkt: RDWD-048WO SEQ ID NO: 5 and SEQ ID NO: 20; SEQ ID NO: 8 and SEQ ID NO: 20; SEQ ID NO: 10 and SEQ ID NO: 20; SEQ ID NO: 2 and SEQ ID NO: 20; SEQ ID NO: 7 and SEQ ID NO: 20; SEQ ID NO: 12 and SEQ ID NO: 20; SEQ ID NO: 1 and SEQ ID NO: 20; or SEQ ID NO: 15 and SEQ ID NO: 20. [0011] In further aspects, the disclosure provides antibodies comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence and the second amino acid sequence are selected from SEQ ID NOs: 1 to 15 and the third amino acid sequence is selected from SEQ ID NOs: 16 to 20. [0012] In certain embodiments, the first amino acid sequence, the second amino acid sequence, and the third amino acid sequence, respectively, comprise: SEQ ID NO: 9, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 18; SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 18; SEQ ID NO: 8, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 3, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 3, SEQ ID NO: 6, and SEQ ID NO: 18; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 16; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 17; SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 16; SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 17; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 19; SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 18; or SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 19. [0013] In some cases, in the subsequence X¹Z¹X²Z²X³Z³ of any one of SEQ ID NOs: 1 to 20: Atty. Dkt: RDWD-048WO X¹ is present or absent, and when present, can be any amino acid; Z¹ is cysteine, serine, 2-formylglycine (fGly), or fGly’, wherein fGly’ is an fGly residue covalently bound to a payload; Z² is proline or alanine; Z³ is an aliphatic amino acid or a basic amino acid; X² and X³ are each independently any amino acid. [0014] In specific embodiments, the subsequence X¹Z¹X²Z²X³Z³ is LCTPSR (SEQ ID NO: 22) or LSTPSR (SEQ ID NO: 23). [0015] In some cases, when Z¹ is fGly’, the antibody is covalently conjugated to a payload via fGly’. The antibody can be covalently conjugated to the first payload via a hydrazone, oxime, semicarbazone, alkyl, alkenyl, acyloxy, hydrazinyl-indolyl, hydrazinyl-imidazoyl, hydrazinyl- pyrrolyl, hydrazinyl-furanyl, or a pyrazalinone linkage. [0016] The first payload can be a small molecule drug, for example, an immunomodulator, a cytotoxic molecule, or a cancer chemotherapeutic agent. [0017] Also provided herein are recombinant nucleic acids comprising nucleotide sequences that encode an antibody described herein. Recombinant expression vectors comprising such nucleic acids are also provided. [0018] Further provided are host cells that are genetically modified to express the antibodies disclosed herein. In certain such embodiments, the host cells are further genetically modified to express a formylglycine generating enzyme (FGE), in a manner sufficient to convert the antibody into an fGly-modified antibody. [0019] Further, provided herein are methods of producing an antibody conjugate, comprising: combining, in a reaction mixture: an antibody disclosed herein, wherein Z¹ is fGly’; and a reactive partner comprising a payload and an aldehyde-reactive group, said combining under conditions sufficient for the aldehyde-reactive group to react with an aldehyde group of the fGly residue thereby conjugating the payload to the fGly residue via a covalent linkage to generate the antibody conjugate; and isolating the antibody conjugate from the reaction mixture. Atty. Dkt: RDWD-048WO [0020] In even further aspects, the disclosure provides formulations comprising an antibody disclosed herein and a pharmaceutically acceptable excipient. [0021] In some aspects, antibodies or formulations described herein can be used to treat a disease in a subject. Such methods comprise administering to a subject a therapeutically effective amount of an antibody, an ADC, or a formulation disclosed herein. In certain such embodiments, the disease is a cancer, an autoimmune disease, or an infection. BRIEF DESCRIPTION OF THE DRAWINGS [0022] FIG.1 provides in vitro potency of anti-HER2 MMAE-conjugated ADCs against NCI-N87 cells. [0023] FIG.2 provides in vitro potency of anti-NaPi2b MMAE-conjugated ADCs against OVCAR3 cells. [0024] FIG.3 provides in vitro potency of anti-NaPi2b belotecan-conjugated ADCs against OVCAR3 cells. [0025] FIG.4 provides in vitro potency of anti-HER2 belotecan-conjugated ADCs against NCI- N87 cells. [0026] FIG.5 provides AC-SINS analysis of anti-HER2 antibodies. [0027] FIG.6 provides AC-SINS analysis of anti-NaPi2b antibodies. [0028] FIG.7 provides melting temperature (Tm1) analysis of anti-HER2 antibodies. [0029] FIG.8 provides melting Temperature (Tm2) analysis of anti-HER2 antibodies. [0030] FIG.9 provides melting temperature (Tm1) analysis of anti-NaPi2b antibodies. [0031] FIG.10 provides insulin polyreactivity analysis of anti-HER2 antibodies. [0032] FIG.11 provides DNA polyreactivity analysis of anti-HER2 antibodies. [0033] FIG.12 provides insulin polyreactivity analysis of anti-NaPi2b antibodies. [0034] FIG.13 provides DNA polyreactivity analysis of anti-NaPi2b antibodies. [0035] FIG.14 shows a schematic of total antibody and total ADC (DAR-sensitive) quantification by ELISA. [0036] FIG.15 shows rat pharmacokinetics for cRW8094: HER2 CH1/CT/22A Compound 43 (Belotecan+iRGD). Atty. Dkt: RDWD-048WO [0037] FIG.16 shows that compound 43 conjugated to CH1/CT/22A- tagged trastuzumab yields a DAR of 5.2 (2.6 belotecan, 2.6 iRGD) as determined by PLRP. [0038] FIG.17 shows that Compound 43 conjugated to CH1/CT/22A- tagged trastuzumab is 97.6% monomeric as determined by analytical SEC. DEFINITIONS [0039] The term “about” as used herein when referring to a measurable value such as an amount, a temporal duration, and the like, is meant to encompass variations of ±20% or ±10%, more preferably ±5%, even more preferably ±1%, and still more preferably ±0.1% from the specified value, as such variations are typical of measurements characterizing the disclosed compositions or appropriate to perform the disclosed methods. [0040] The terms “polypeptide,” “peptide,” and “protein” are used interchangeably herein to refer to a polymeric form of amino acids of any length. Unless specifically indicated otherwise, “polypeptide,” “peptide,” and “protein” can include genetically coded and non- coded amino acids, chemically or biochemically modified or derivatized amino acids, and polypeptides having modified peptide backbones. The term includes fusion proteins, including, but not limited to, fusion proteins with a heterologous amino acid sequence, fusions with heterologous and homologous leader sequences, proteins which contain at least one N- terminal methionine residue (e.g., to facilitate production in a recombinant bacterial host cell); immunologically tagged proteins; and the like. [0041] “Native amino acid sequence” or “parent amino acid sequence” are used interchangeably herein in the context of an immunoglobulin to refer to the amino acid sequence of the immunoglobulin prior to modification to include a heterologous aldehyde tag. [0042] The term "antibody" is used in the broadest sense and includes monoclonal antibodies, and multispecific antibodies (e.g., bispecific antibodies), humanized antibodies, chimeric antibodies, and antigen-binding antibody fragments (e.g., Fab fragments). A target antigen can have one or more binding sites, also called epitopes, recognized by complementarity determining regions (CDRs) formed by one or more variable regions of an antibody. Atty. Dkt: RDWD-048WO [0043] “Bind” as used in reference to an antibody may refer to the physical interaction between an antibody and a target (e.g., an antigen) characterized by an affinity (K_D) value of 10^-6 M or less, e.g., 10^-7 M or less, 10^-8 M or less, 10^-9 M or less, 10^-10 M or less, including 10^-11 M or less. A lower K_D value corresponds to a higher binding affinity (i.e., stronger binding) so that a K_D value of 10^-7 M indicates a higher binding affinity than a K_D value of 10^-6 M. [0044] “Immunoglobulin” as used herein refers to a polypeptide comprising at least a constant region of a light chain or at least a constant region of a heavy chain. [0045] An immunoglobulin light or heavy chain variable region is composed of a framework region (FR) interrupted by three hypervariable regions, also called “complementarity determining regions” or “CDRs.” The extent of the framework region and CDRs have been defined (see, “Sequences of Proteins of Immunological Interest,” E. Kabat et al., U.S. Department of Health and Human Services, 1991). The framework region of an antibody, which is the combined framework regions of the constituent light and heavy chains, serves to position and align the CDRs. The CDRs are primarily responsible for binding to an epitope of an antigen. An immunoglobulin light chain may have a structure schematically represented, from N- to C-termini, as: FR1-CDR1-FR2-CDR2-FR3-CDR3-FR4-CL, where CDR1, CDR2 and CDR3 are hypervariable regions that interrupt the framework region into four (FR1, FR2, FR3 and FR4) and CL is the constant region. An immunoglobulin heavy chain may have a structure schematically represented, from N- to C-termini, as: FR1-CDR1-FR2-CDR2-FR3-CDR3- FR4-CH1-H-CH2-CH3, where CDR1, CDR2 and CDR3 are hypervariable regions that interrupt the framework region into four (FR1, FR2, FR3 and FR4), CH1, CH2 and CH3 are constant regions and H is a hinge region. [0046] The term “natural antibody” refers to an antibody in which the heavy and light chains of the antibody have been made and paired by the immune system of a multi-cellular organism. Spleen, lymph nodes, bone marrow and serum are examples of tissues that produce natural antibodies. For example, the antibodies produced by the antibody producing cells isolated from an animal immunized with an antigen are natural antibodies. [0047] A “parent Ig” is a polypeptide comprising an amino acid sequence which lacks a tag as described herein. The parent Ig may comprise a native sequence constant region, or Atty. Dkt: RDWD-048WO may comprise a constant region with pre-existing amino acid sequence modifications (such as additions, deletions and/or substitutions). [0048] In the context of an Ig, the term “constant region” is well understood in the art, and refers to a C-terminal region of an Ig heavy chain, or an Ig light chain. An Ig heavy chain constant region includes CH1, CH2, and CH3 domains (and CH4 domains, where the heavy chain is a μ or an ε heavy chain). In a native Ig heavy chain, the CH1, CH2, CH3 (and, if present, CH4) domains begin immediately after (C-terminal to) the heavy chain variable (V_H) region, and are each from about 100 amino acids to about 130 amino acids in length. In a native Ig light chain, the constant region begins immediately after (C-terminal to) the light chain variable (VL) region, and is about 100 amino acids to 120 amino acids in length. [0049] In some embodiments, a “functional Fc region” possesses an “effector function” of a native sequence Fc region. Exemplary “effector functions” include C1q binding; complement dependent cytotoxicity; Fc receptor binding; antibody-dependent cell-mediated cytotoxicity (ADCC); phagocytosis; down-regulation of cell surface receptors (e.g. B cell receptor; BCR), etc. Such effector functions generally require the Fc region to be combined with a binding domain (e.g. an antibody variable domain) and can be assessed using various assays that are well known in the art. [0050] “Antibody-dependent cell-mediated cytotoxicity” and “ADCC” refer to a cell- mediated reaction in which nonspecific cytotoxic cells that express FcRs (e.g. Natural Killer (NK) cells) recognize bound antibody on a target cell and subsequently cause lysis of the target cell. The primary cells for mediating ADCC, NK cells, express FcγRIII only, whereas monocytes express FcγRI, FcγRII and FcγRIII. The terms “Fc receptor” or “FcR” are used to describe a receptor that binds to the Fc region of an antibody. [0051] The term “humanized antibody” or “humanized immunoglobulin” refers to a non-human (e.g., mouse or rabbit) antibody containing one or more amino acids (in a framework region, a constant region or a CDR, for example) that have been substituted with a correspondingly positioned amino acid from a human antibody. In general, humanized antibodies produce a reduced immune response in a human host, as compared to a non- humanized version of the same antibody. Antibodies can be humanized using a variety of techniques known in the art including, for example, CDR-grafting, veneering or resurfacing, and Atty. Dkt: RDWD-048WO chain shuffling. In certain embodiments, framework substitutions are identified by modeling of the interactions of the CDR and framework residues to identify framework residues important for antigen binding and sequence comparison to identify unusual framework residues at particular positions. [0052] The term “chimeric antibodies” refer to antibodies whose light and heavy chain genes have been constructed, typically by genetic engineering, from antibody variable and constant region genes belonging to different species. For example, the variable segments of the genes from a mouse monoclonal antibody may be joined to human constant segments, such as gamma 1 and gamma 3. An example of a therapeutic chimeric antibody is a hybrid protein composed of the variable or antigen-binding domain from a mouse antibody and the constant or effector domain from a human antibody, although domains from other mammalian species may be used. [0053] By “genetically-encodable” as used in reference to an amino acid sequence of polypeptide, peptide or protein means that the amino acid sequence is composed of amino acid residues that are capable of production by transcription and translation of a nucleic acid encoding the amino acid sequence, where transcription and/or translation may occur in a cell or in a cell-free in vitro transcription/translation system. [0054] The term “control sequences” refer to DNA sequences that facilitate expression of an operably linked coding sequence in a particular expression system, e.g. mammalian cell, bacterial cell, cell-free synthesis, etc. The control sequences that are suitable for prokaryote systems, for example, include a promoter, optionally an operator sequence, and a ribosome binding site. Eukaryotic cell systems may utilize promoters, polyadenylation signals, and enhancers. [0055] A nucleic acid is “operably linked” when it is placed into a functional relationship with another nucleic acid sequence. For example, DNA for a presequence or secretory leader is operably linked to DNA for a polypeptide if it is expressed as a preprotein that participates in the secretion of the polypeptide; a promoter or enhancer is operably linked to a coding sequence if it affects the transcription of the sequence; or a ribosome binding site is operably linked to a coding sequence if it is positioned so as to facilitate the initiation of translation. Generally, “operably linked” means that the DNA sequences being linked are Atty. Dkt: RDWD-048WO contiguous, and, in the case of a secretory leader, contiguous and in reading frame. Linking is accomplished by ligation or through amplification reactions. Synthetic oligonucleotide adaptors or linkers may be used for linking sequences in accordance with conventional practice. [0056] The term “expression cassette” as used herein refers to a segment of nucleic acid, usually DNA that can be inserted into a nucleic acid (e.g., by use of restriction sites compatible with ligation into a construct of interest or by homologous recombination into a construct of interest or into a host cell genome). In general, the nucleic acid segment comprises a polynucleotide that encodes a polypeptide of interest (e.g., a tagged Ig protein), and the cassette and restriction sites are designed to facilitate insertion of the cassette in the proper reading frame for transcription and translation. Expression cassettes can also comprise elements that facilitate expression of a polynucleotide encoding a polypeptide of interest in a host cell. These elements may include, but are not limited to: a promoter, a minimal promoter, an enhancer, a response element, a terminator sequence, a polyadenylation sequence, and the like. [0057] As used herein the term “isolated” is meant to describe a compound of interest that is in an environment different from that in which the compound naturally occurs. “Isolated” is meant to include compounds that are within samples that are substantially enriched for the compound of interest and/or in which the compound of interest is partially or substantially purified. [0058] As used herein, the term “substantially purified” refers to a compound that is removed from its natural environment and is at least 60% free, at least 75% free, at least 80% free, at least 85% free, at least 90% free, at least 95% free, at least 98% free, or more than 98% free, from other components with which it is naturally associated. [0059] The term “physiological conditions” is meant to encompass those conditions compatible with living cells, e.g., predominantly aqueous conditions of a temperature, pH, salinity, etc. that are compatible with living cells. [0060] “N-terminus” refers to the terminal amino acid residue of a polypeptide having a free amine group, which amine group in non-N-terminus amino acid residues normally forms part of the covalent backbone of the polypeptide. Atty. Dkt: RDWD-048WO [0061] “C-terminus” refers to the terminal amino acid residue of a polypeptide having a free carboxyl group, which carboxyl group in non-C-terminus amino acid residues normally forms part of the covalent backbone of the polypeptide. [0062] By “internal site” as used in referenced to a polypeptide or an amino acid sequence of a polypeptide means a region of the polypeptide that is not at the N-terminus or at the C- terminus. [0063] As used herein, the terms “treat,” “treatment,” “treating,” and the like, refer to obtaining a desired pharmacologic and/or physiologic effect. The effect may be prophylactic in terms of completely or partially preventing a disease or symptom thereof and/or may be therapeutic in terms of a partial or complete cure for a disease and/or adverse effect attributable to the disease. “Treatment,” as used herein, covers any treatment of a disease in a mammal, particularly in a human, and includes: (a) inhibiting the disease, i.e., arresting its development; and (b) relieving the disease, e.g., causing regression of the disease, e.g., to completely or partially remove symptoms of the disease. [0064] The term “prevent,” “prevention,” or “preventing” as it relates to a disease refers to preventing the disease from occurring in a subject, who may be predisposed to the disease but has not yet been diagnosed as having it. [0065] A “therapeutically effective amount” refers to an amount effective, at dosages and for periods of time necessary, to achieve the desired therapeutic result, such as treatment or prevention. A therapeutically effective amount of a therapeutic agent may vary according to factors such as the disease state, age, sex, and weight of the individual, and the ability of the therapeutic agent to elicit a desired response in the individual. A therapeutically effective amount is also one in which any toxic or detrimental effects of the therapeutic agent are outweighed by the therapeutically beneficial effects. [0066] The term “tag” as used herein refers to an amino acid sequence that contains an amino acid sequence motif found in sulfatases (hereinafter “sulfatase motif”), which amino acid sequence motif is capable of being converted, by action of an FGE, to contain a 2- formylglycine residue (referred to herein as “fGly”). The fGly residue generated by an FGE is often referred to in the literature as a “formylglycine.” Stated differently, the term “tag” is used herein to refer to an amino acid sequence comprising an “unconverted” sulfatase motif (i.e., a Atty. Dkt: RDWD-048WO sulfatase motif in which the cysteine or serine residues has not been converted to fGly by an FGE, but is capable of being converted). The sulfatase motif may be exchangeable with “FGE substrate motif.” A “tagged” polypeptide contains an amino acid sequence motif, e.g., a sulfatase motif, which can be converted by an FGE to contain fGly. [0067] By “conversion” as used in the context of action of an FGE on a sulfatase motif refers to biochemical modification of a cysteine or serine residue in a sulfatase motif to an fGly residue (e.g., Cys to fGly, or Ser to fGly). [0068] “Aldehyde tag” or “ald-tag” as used herein, may refer to a tag that contains a sulfatase motif, which has been converted, by action of an FGE, to contain fGly. A converted tag refers to an amino acid sequence comprising a “converted” sulfatase motif (i.e., a sulfatase motif in which the cysteine or the serine residue has been converted to fGly by action of an FGE). An “aldehyde tagged” polypeptide contains an amino acid sequence motif, e.g., a sulfatase motif that has been converted by an FGE to contain fGly. [0069] The term “reactive partner” means a molecule or molecular moiety that specifically reacts with another reactive partner to produce a reaction product. Exemplary reactive partners include a cysteine or serine of sulfatase motif and an FGE, which react to form a reaction product of a converted aldehyde tag containing an fGly in lieu of cysteine or serine in the motif. Other exemplary reactive partners include an aldehyde of an fGly residue of a converted aldehyde tag and an “aldehyde-reactive reactive partner,” which comprises an aldehyde-reactive group and a moiety of interest (i.e., a payload, e.g., drug), and which reacts to form a reaction product of a modified aldehyde tagged polypeptide having the payload (e.g., drug) conjugated to the fGly-modified polypeptide via an fGly residue. [0070] The term “conjugate” means that a first moiety is stably associated with a second moiety. The term “stably associated” means that a moiety is bound to another moiety or structure under standard conditions. In certain embodiments, the first and second moieties are bound to each other through one or more covalent bonds. The first or the second moiety of a conjugate may be referred to as a “payload.” [0071] Before the present disclosure is further described, it is to be understood that the disclosed subject matter is not limited to particular embodiments described, as such may, of course, vary. It is also to be understood that the terminology used herein is for the purpose of Atty. Dkt: RDWD-048WO describing particular embodiments only, and is not intended to be limiting, since the scope of the present disclosure will be limited only by the appended claims. [0072] Where a range of values is provided, it is understood that each intervening value, to the tenth of the unit of the lower limit unless the context clearly dictates otherwise, between the upper and lower limit of that range and any other stated or intervening value in that stated range, is encompassed within the disclosed subject matter. The upper and lower limits of these smaller ranges may independently be included in the smaller ranges, and are also encompassed within the disclosed subject matter, subject to any specifically excluded limit in the stated range. Where the stated range includes one or both of the limits, ranges excluding either or both of those included limits are also included in the disclosed subject matter. [0073] Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the disclosed subject matter belongs. Although any methods and materials similar or equivalent to those described herein can also be used in the practice or testing of the disclosed subject matter, the preferred methods and materials are now described. All publications mentioned herein are incorporated herein by reference to disclose and describe the methods and/or materials in connection with which the publications are cited. [0074] It must be noted that as used herein and in the appended claims, the singular forms “a,” “an,” and “the” include plural referents unless the context clearly dictates otherwise. Thus, for example, reference to “an antibody” includes a plurality of such antibodies and reference to “the antigen” includes reference to one or more antigens and equivalents thereof known to those skilled in the art, and so forth. It is further noted that the claims may be drafted to exclude any optional element. As such, this statement is intended to serve as antecedent basis for use of such exclusive terminology as “solely,” “only” and the like in connection with the recitation of claim elements, or use of a “negative” limitation. [0075] It is appreciated that certain features of the disclosed subject matter, which are, for clarity, described in the context of separate embodiments, may also be provided in combination in a single embodiment. Conversely, various features of the disclosed subject matter, which are, for brevity, described in the context of a single embodiment, may also be provided separately or in any suitable sub-combination. All combinations of the embodiments Atty. Dkt: RDWD-048WO pertaining to the disclosure are specifically embraced by the disclosed subject matter and are disclosed herein just as if each and every combination was individually and explicitly disclosed. In addition, all sub-combinations of the various embodiments and elements thereof are also specifically embraced by the present disclosure and are disclosed herein just as if each and every such sub-combination was individually and explicitly disclosed herein. [0076] The publications discussed herein are provided solely for their disclosure prior to the filing date of the present application. Nothing herein is to be construed as an admission that the disclosed subject matter is not entitled to antedate such publication by virtue of prior invention. Further, the dates of publication provided may be different from the actual publication dates which may need to be independently confirmed. DETAILED DESCRIPTION [0077] In certain aspects, the disclosure provides antibodies and ADCs with improved production outcomes and that enable the production of unanticipated and unexpected molecular compositions with novel functionalities. The antibodies and ADCs disclosed herein are generated using site-specific conjugation facilitated by the aldehyde tag. In this approach, an aldehyde functional group is installed at a desired location within the antibody by genetically-engineering a short consensus sequence recognized by FGE. During protein production, when an antibody expressed in a cell line that overexpresses FGE, a cysteine in the consensus sequence is converted to an fGly that contains an aldehyde. The aldehyde is chemically biorthogonal to other functional groups within the protein and serves as the handle for site-specific bioconjugation. Various conjugation chemistries can be used to ligate a linker- payload to the aldehyde-containing antibody. Such chemistries include Knoevenagel condensation (or trapped-Knoevenagel), oxime/hydrazone ligation, strain-promoted alkyne- nitrone cycloaddition, Mukaiyama aldol reaction, Wittig reaction, indium-mediated allylation, and HIPS ligation (Hydrazino-Iso-Pictet-Spengler), which has risen to be the most practical and scalable of all methods. Certain such conjugation methods and chemistries are described in Huang et al. (2018) mAbs.10:1182-1189; Drake et al. (2014) Bioconjugate Chemistry, 25:1331- 1341, and U.S. Patent Nos.9,310,374, 9,493,413, 10,344,311, 11,466,096, and 11,208,632, which are herein incorporated by reference in their entireties. Atty. Dkt: RDWD-048WO [0078] Aldehyde-tagged antibodies can be made with the tag site in a limited set of locations that allow the for efficient antibody and ADC production (encompassing protein production and purification, bioconjugation followed by purification, and a final molecule displaying acceptable DAR and biophysical properties). To achieve this at a manufacturing scale with a reasonable cost-of-goods, certain critical quality attributes are defined for the tag site, protein, and conjugate. For example, titers must be acceptable. Next, conversion of the aldehyde tag from cysteine to fGly must be efficient, with ≤ 5% unconverted cysteine remaining in the protein at each tag site. Then, desired DAR values should be achievable. Finally, the ADC preparation must have good biophysical characteristics, for example, by showing minimal aggregation or truncation or fragmentation. A cutoff of ≤ 5% high- or low-molecular weight species is generally used as a metric for aldehyde tag/linker-payload screening and discovery efforts. [0079] When considering the insertion and conjugation of a single aldehyde tag into a protein, or specifically, into an antibody, it is very difficult to predict successful tag locations. Instead, successful tag locations have been identified empirically. [0080] Considering the challenges for making single-tagged antibodies and ADCs, identifying tag locations that combine well together to produce double-tagged or triple-tagged antibodies and ADCs with the desired biophysical, functional, and manufacturability properties poses an even higher hurdle. However, double and triple-tagged antibodies and ADCs are desirable for generating higher DAR conjugates, which are of ever-increasing therapeutic interest due to the desirability of some lower-potency payloads (such as camptothecins and protein degraders). Also, having access to tag locations suitable for producing double or triple tag antibodies facilitates producing antibodies with multiple tags combinations that can yield manufacturable ADCs. In addition to manufacturability, access to tag sites suitable for producing double or triple tag combinations enable the generation of ADCs with superior properties. [0081] The disclosure describes manufacturability characteristics of antibodies and ADCs made with over 40 double tag combinations, with more than 20 combinations tested in two or more parental antibodies, such as trastuzumab, polatuzumab, and gemtuzumab, and their variants. Several of the tested combinations showed desirable manufacturability characteristics, as shown in Tables 1-8. Atty. Dkt: RDWD-048WO [0082] Also, certain triple tagged antibodies were produced by accident as described in Example 2 below. However, based on the surprising success of such accidentally produced triple tagged antibodies, additional such triple tagged antibodies were produced and tested. [0083] Accordingly, the disclosure describes antibodies that include two or more tags containing a sulfatase motif in an Ig heavy chain and/or an Ig light chain. The tag includes a substrate motif for an FGE, where FGE can convert (oxidize) a serine or cysteine residue in the substrate motif to fGly, thereby generating an fGly-modified antibody. An fGly-modified antibody can further react with an aldehyde-reactive partner to generate an antibody conjugate, where a moiety of interest (i.e., a payload, e.g., drug) is covalently bound with site- specificity to the heavy and/or the light chain via the fGly. [0084] The tagged antibodies, conjugates, compositions and methods of the present disclosure exploit a naturally-occurring, genetically-encodable sulfatase motif for use as a tag to direct site-specific modification of an Ig. The sulfatase motif of the tag, which motif is based on a motif found in active sites of sulfatases, contains a serine or cysteine residue that is capable of being converted (oxidized) to fGly residue by action of an FGE either in a cell-based system in an FGE-expressing host cell (e.g., at the time of translation of an ald tag-containing protein in a cell) or in a cell-free system (e.g., by contacting an ald tag-containing protein with an FGE in a cell-free system). The aldehyde moiety of the resulting fGly residue can be used as a “chemical handle” to facilitate site-specific chemical modification of the Ig, and thus site-specific attachment of a payload (e.g., drug). For example, a peptide modified to contain an α- nucleophile-containing moiety (e.g., an aminooxy or hydrazide moiety) can be reacted with the fGly-containing Ig to yield a conjugate in which the Ig and the peptide are linked by a covalent bond, e.g., a hydrazone or oxime bond, or via alternative aldehyde-specific chemistries such as reductive amination, etc. The reactivity of the aldehyde thus allows for bioorthogonal and chemoselective modification of the Ig, and thus provides a site-specific means for chemical modification that in turn can be exploited to provide for site-specific attachment of a payload in the final conjugate. [0085] The two or more tags can be positioned in an Ig heavy chain and/or an Ig light chain in any suitable manner, as described herein. Atty. Dkt: RDWD-048WO [0086] The tags may be positioned in an Ig heavy chain and/or a light chain in any suitable manner such that the tagged heavy chain and/or the tagged antibody having the tagged heavy and/or the light chains exhibit one or more desirable properties. These properties may be associated with, e.g., the tagged and/or the fGly-modified antibody produced in vitro (i.e., in a cellular expression system); and/or the antibody conjugate having a payload (e.g., drug) covalently bound to the antibody through fGly. [0087] The desirable properties may include, without limitation, higher titer of antibody production, higher conversion rate, higher conjugation yield (or conjugation efficiency) (e.g., as measured by the average molar ratio of payload to antibody, e.g., drug to antibody), lower aggregation rate (or higher percentage of antibody monomers), lower immunogenicity; and/or higher stability in serum relative to reference measures for the respective properties. A tagged, fGly-modified or conjugated antibody of the present disclosure may be characterized in satisfying one or more threshold criteria, e.g., two or more threshold criteria, such as expression titer and/or conjugation yield (e.g., payload-to-antibody ratio (PAR), e.g., the drug- to-antibody ratio, or DAR, where the payload is a drug) that are higher than a threshold titer and/or a threshold yield, respectively. [0088] A tagged or fGly-modified antibody of the present disclosure may exhibit a desirable titer of expression. “Titer of expression,” “expression titer,” and “titer” are used herein interchangeably, in reference to an antibody, to refer to the amount of antibody secreted in a cell culture supernatant by cultured cells that are genetically modified with suitable expression constructs encoding the antibody. The cells may be genetically modified to co-express any tagged or untagged Ig light chain with a tagged Ig heavy chain. The cells may be further genetically modified with additional expression constructs encoding enzymes, or any other suitable polypeptide. In some cases, the cells may be genetically modified to express an FGE, as described herein. The threshold titer of expression may be, in some cases, about 20 mg/L or more, e.g., 30 mg/L or more, 40 mg/L or more, 50 mg/L or more, about 75 mg/L or more, about 100 mg/L or more, about 150 mg/L or more, about 200 mg/L or more, about 300 mg/L or more, about 400 mg/L or more, about 500 mg/L or more, about 600 mg/L or more, about 700 mg/L or more, about 800 mg/L or more, including about 1,000 mg/L or more. In some embodiments, the threshold titer of expression is in the range of about 20 mg/L to about 2,000 Atty. Dkt: RDWD-048WO mg/L, e.g., about 30 mg/L to about 2,000 mg/L, about 50 mg/L to about 2,000 mg/L, about 100 mg/L to about 1,800 mg/L, about 200 mg/L to about 1,600 mg/L, about 300 mg/L to about 1,500 mg/L, or about 400 mg/L to about 1,500 mg/L. The antibody titer may be measured using, e.g., a biosensor chip system, such as a protein A-based biosensor assay run on the BLItz® system (Forte Bio, CA). [0089] An fGly-modified antibody that includes converted tags present in an Ig heavy chain and/or a light chain constant region, as disclosed herein, may exhibit a desirable conjugation efficiency, as expressed by the average molar ratio of payload to antibody (PAR) (e.g., drug- antibody ratio (DAR), where the payload is a drug), when the fGly-modified antibody is conjugated with a payload, such as a drug, through the fGly in a suitable reaction mixture. The payload prior to conjugation with the fGly-modified antibody may be covalently attached to a suitable reactive group, e.g., an aldehyde-reactive group, which reacts with the aldehyde of the fGly residue of the fGly-modified antibody in the reaction mixture under suitable conditions. In some embodiments, the conjugation efficiency is about 0.5 or more per tag, e.g., about 0.75 or more per tag, about 1.0 or more per tag, about 1.1 or more per tag, about 1.2 or more per tag, about 1.3 or more per tag, about 1.6 or more per tag, about 1.7 or more per tag, about 1.8 or more per tag, and up to 2.0 per tag. In some embodiments, the conjugation efficiency is in the range of about 0.5 to about 2.0 per tag, e.g., about 0.75 to about 2.0 per tag, about 1.0 to about 1.9 per tag, about 1.3 to about 1.9 per tag, or about 1.6 to 1.8 per tag. The conjugation yield may be measured by performing, e.g., hydrophobic interaction chromatography (HIC), after a conjugation reaction. [0090] An antibody conjugate of the present disclosure (e.g., an antibody having two or more payload molecules, such as a drug, covalently bound thereto through an fGly of an aldehyde- tagged Ig heavy chain constant region of the antibody) may show an acceptable level of aggregation, as represented by the proportion of antibody monomers. “Antibody monomer,” as used herein, may refer to an antigen-binding unit containing, e.g., a pair of Ig light chain and a pair of Ig heavy chains. Aggregation occurs when more than one antibody monomers associate together (and therefore are no longer antibody monomers). Thus, two or more antibody monomers can associate with each other to form an aggregate. The proportion of Atty. Dkt: RDWD-048WO antibody monomers may be affected by the aggregation of antibody monomers as well as disassociation of one of more Ig of an antibody monomer. [0091] In certain embodiments, the proportion of antibody monomers is about 20% or more, e.g., about 30% or more, about 40% or more, about 50% or more, about 60% or more, about 70% or more, about 80% or more, about 90% or more, including about 95% or more. In some cases, the percentage of antibody monomers is in the range of from about 20% to about 99%, e.g., from about 30% to about 99%, from about 40% to about 99%, from about 50% to about 99%, from about 60% to about 98%, from about 70% to about 98%, from about 80% to about 98%, including from about 90% to about 98%. The proportion of antibody monomers may be measured using, e.g., size exclusion chromatography. [0092] An antibody conjugate of the present disclosure may bind an antigen with a suitable binding activity (e.g., specificity, binding affinity, etc.) compared to the parent antibody (i.e., the antibody without a payload conjugated thereto, or the antibody having an Ig heavy chain and/or a light chain without the tag sequence inserted in the constant region). In some cases, the antibody conjugate has binding activity toward an antigen that is substantially the same as the binding activity of a parent antibody that does not have a tag sequence inserted in the constant region of the Ig heavy chain and/or a light chain antibody. The binding activity may be measured by, e.g., an enzyme-linked immunosorbent assay (ELISA). [0093] The present antibody conjugates may find use in delivering a conjugated payload (e.g., drug) to a target site, where the antibody conjugate may bind specifically to an antigen specific for, or enriched at, the target site. For example, the antibody conjugate may specifically recognize a tumor antigen and enhance site-specific delivery of a chemotherapeutic drug conjugated to the antibody to the tumor. [0094] Further aspects of the present disclosure are now described. T^AGS C^{ONTAINING A} S^ULFATASE M^OTIF [0095] An antibody of the present disclosure includes a tag, i.e., includes an amino acid sequence containing a sulfatase motif which is capable of being converted, by action of FGE, to provide an fGly in the sulfatase motif, in an Ig heavy chain constant region and/or an Ig light chain constant region. The tag may include a sulfatase motif having a length of 5 amino acid Atty. Dkt: RDWD-048WO residues or more, e.g., 6 amino acid residues or more, 7 amino acid residues or more, 8 amino acid residues or more, including 10 amino acid residues or more, and in some cases may have a length of 15 amino acid residues or less, e.g., 12 amino acid residues or less, 11 amino acid residues or less, 10 amino acid residues or less, including 8 amino acid residues or less. In some embodiments, the tag includes a sulfatase motif having a length in the range of 5 to 15 amino acid residues, e.g., 5 to 12 amino acid residues, 5 to 10 amino acid residues, including 6 to 8 residues. In some embodiments, the sulfatase motif includes 5 or 6 amino acid residues. [0096] In some embodiments, the tag includes at least a minimal sulfatase motif (also referred to a “consensus sulfatase motif”), having 5 or 6 amino acid residues, and additional sequence flanking the minimal sulfatase motif. The additional sequence may be N- and/or C-terminal to the minimal sulfatase motif. [0097] In certain embodiments, the sulfatase motif may be described by the formula: X¹Z¹X²Z²X³Z³ (I) where Z¹ is cysteine or serine (which can also be represented by (C/S)); Z² is either a proline or alanine residue (which can also be represented by (P/A)); Z³ is a basic amino acid (e.g., arginine (R), and may be lysine (K) or histidine (H), usually lysine), or an aliphatic amino acid (alanine (A), glycine (G), leucine (L), valine (V), isoleucine (I), or proline (P), usually A, G, L, V, or I; X¹ is present or absent and, when present, can be any amino acid, though usually an aliphatic amino acid, a sulfur-containing amino acid, or a polar, uncharged amino acid, (i.e., other than an aromatic amino acid or a charged amino acid), usually L, M, V, S or T, more usually L, M, S or V; and X² and X³ independently can be any amino acid, though usually an aliphatic amino acid, a polar, uncharged amino acid, or a sulfur containing amino acid (i.e., other than an aromatic amino acid or a charged amino acid), usually S, T, A, V, G or C, more usually S, T, A, V or G. [0098] Thus, the present disclosure provides an antibody, where the Ig heavy chain and/or the Ig light chain of the antibody includes a constant region amino acid sequence modified to provide two or more tags having at least 5 amino acids and having the formula X¹Z¹X²Z²X³Z³, where Z¹ is cysteine or serine; Z² is a proline or alanine residue; Z³ is an aliphatic amino acid or a basic amino acid; X¹ is present or absent and, when present, is any amino acid; X² and X³ are each independently any amino acid. Atty. Dkt: RDWD-048WO [0099] Following action of an FGE on the sulfatase motif, Z¹ is oxidized to generate an fGly residue. Further, following both FGE-mediated conversion and reaction with a reactive partner comprising a moiety of interest (i.e., a payload, e.g., drug, detectable label, water soluble polymer, polypeptide, etc.), fGly position at Z¹ in the formula above is covalently bound to the payload. [00100] The sulfatase motif of the tag is generally selected so as to be capable of conversion by a selected FGE, e.g., an FGE present in a host cell in which the antibody of the present disclosure is expressed or an FGE which is to be contacted with the antibody of the present disclosure in a cell-free, in vitro method. [00101] Selection of tags and an FGE that provide for conversion of a tag to include an fGly in the target antibody containing a tagged Ig heavy chain can be readily accomplished in light of information available in the art, for example, in the U.S. Patent Nos.11,466,096 and 11,208,632, which are herein incorporated by reference in their entireties. [00102] In general, sulfatase motifs susceptible to conversion by a eukaryotic FGE contain a cysteine and a proline (i.e., a cysteine and proline at Z¹ and Z², respectively, in Formula I above (e.g., X¹CX²PX³Z³) and are modified by the “SUMF1-type” FGE (Cosma et al. Cell 2003, 113, (4), 445-56; Dierks et al. Cell 2003, 113, (4), 435-44). Sulfatase motifs susceptible to conversion by a prokaryotic FGE contain either a cysteine or a serine, and a proline in the sulfatase motif (i.e., a cysteine or serine at Z¹, and a proline at Z², respectively, in Formula I above (e.g., X¹(C/S)X²PX³Z³) are modified either by the “SUMF1-type” FGE or the “AtsB-type” FGE, respectively (Szameit et al. J Biol Chem 1999, 274, (22), 15375-81). Other sulfatase motifs susceptible to conversion by a prokaryotic FGE contain either a cysteine or a serine, and either a proline or an alanine in the sulfatase motif (i.e., a cysteine or serine at Z¹, and a proline or alanine at Z2, respectively, in Formula I above or Formula II described elsewhere in this disclosure (e.g., X¹CX²PX³R; X¹SX²PX²R; X¹CX²AX³R; X¹SX²AX³R; CX¹PX²R; SX¹PX²R; CX¹AX²R; SX¹AX²R, X¹CX²PX³Z³; X¹SX²PX² Z³; X¹CX²AX³Z³; X¹SX²AX³Z³; CX¹PX²Z³; SX¹PX²Z³; CX¹AX²Z³; SX¹AX²Z³), and are susceptible to modification by, for example, can be modified by an FGE of a Firmicutes (e.g., Clostridium perfringens) (see Berteau et al. J. Biol. Chem.2006; 281:22464-22470) or an FGE of Mycobacterium tuberculosis. Atty. Dkt: RDWD-048WO [00103] Therefore, for example, where the FGE is a eukaryotic FGE (e.g., a mammalian FGE, including a human FGE), the sulfatase motif is usually of the formula: X¹CX²PX³Z³, where X¹ may be present or absent and, when present, can be any amino acid, though usually an aliphatic amino acid, a sulfur-containing amino acid, or a polar, uncharged amino acid, (i.e., other than an aromatic amino acid or a charged amino acid), usually L, M, S or V; X² and X³ independently can be any amino acid, though usually an aliphatic amino acid, a sulfur- containing amino acid, or a polar, uncharged amino acid, (i.e., other than an aromatic amino acid or a charged amino acid), usually S, T, A, V, G, or C, more usually S, T, A, V or G; and Z³ is a basic amino acid (e.g., arginine (R), and may be lysine (K) or histidine (H), usually lysine), or an aliphatic amino acid (alanine (A), glycine (G), leucine (L), valine (V), isoleucine (I), or proline (P), usually A, G, L, V, or I. [00104] Specific examples of sulfatase motifs include LCTPSR (SEQ ID NO: 22) or LSTPSR (SEQ ID NO: 23), MCTPSR (SEQ ID NO: 24), VCTPSR (SEQ ID NO: 25), LCSPSR (SEQ ID NO: 26), LCAPSR (SEQ ID NO: 27), LCVPSR (SEQ ID NO: 28), LCGPSR (SEQ ID NO: 29), ICTPAR (SEQ ID NO: 30), LCTPSK (SEQ ID NO: 31), MCTPSK (SEQ ID NO: 32), VCTPSK (SEQ ID NO: 33), LCSPSK (SEQ ID NO: 34), LCAPSK (SEQ ID NO: 35), LCVPSK (SEQ ID NO: 36), LCGPSK (SEQ ID NO: 37), LCTPSA (SEQ ID NO: 38), ICTPAA (SEQ ID NO: 39), MCTPSA (SEQ ID NO: 40), VCTPSA (SEQ ID NO: 41), LCSPSA (SEQ ID NO: 42), LCAPSA (SEQ ID NO: 43), LCVPSA (SEQ ID NO: 44), LCGPSA (SEQ ID NO: 45), MSTPSR (SEQ ID NO: 46), VSTPSR (SEQ ID NO: 47), LSSPSR (SEQ ID NO: 48), LSAPSR (SEQ ID NO: 49), LSVPSR (SEQ ID NO: 50), LSGPSR (SEQ ID NO: 51), ISTPAR (SEQ ID NO: 52), LSTPSK (SEQ ID NO: 53), MSTPSK (SEQ ID NO: 54), VSTPSK (SEQ ID NO: 55), LSSPSK (SEQ ID NO: 56), LSAPSK (SEQ ID NO: 57), LSVPSK (SEQ ID NO: 58), LSGPSK (SEQ ID NO: 59), LSTPSA (SEQ ID NO: 60), ISTPAA (SEQ ID NO: 61), MSTPSA (SEQ ID NO: 62), VSTPSA (SEQ ID NO: 63), LSSPSA (SEQ ID NO: 64), LSAPSA (SEQ ID NO: 65), LSVPSA (SEQ ID NO: 66), and LSGPSA (SEQ ID NO: 67). Other specific sulfatase motifs are readily apparent from the disclosure provided herein. [00105] In certain such cases, when the Z¹ residue of the sulfatase motif is converted to fGly, it produces a sequence of M(fGly)TPSR (SEQ ID NO: 68), V(fGly)TPSR (SEQ ID NO: 69), L(fGly)SPSR (SEQ ID NO: 70), L(fGly)APSR (SEQ ID NO: 71), L(fGly)VPSR (SEQ ID NO: 72), L(fGly)GPSR (SEQ ID NO: 73), I(fGly)TPAR (SEQ ID NO: 74), L(fGly)TPSK (SEQ ID NO: 75), M(fGly)TPSK (SEQ ID NO: 76), V(fGly)TPSK (SEQ ID NO: 77), L(fGly)SPSK (SEQ ID NO: 78), Atty. Dkt: RDWD-048WO L(fGly)APSK (SEQ ID NO: 79), L(fGly)VPSK (SEQ ID NO: 80), L(fGly)GPSK (SEQ ID NO: 81), L(fGly)TPSA (SEQ ID NO: 82), I(fGly)TPAA (SEQ ID NO: 83), M(fGly)TPSA (SEQ ID NO: 84), V(fGly)TPSA (SEQ ID NO: 85), L(fGly)SPSA (SEQ ID NO: 86), L(fGly)APSA (SEQ ID NO: 87), L(fGly)VPSA (SEQ ID NO: 88), L(fGly)GPSA (SEQ ID NO: 89), and L(fGly)TPSR (SEQ ID NO: 90). ANTIBODIES WITH A TAGGED IMMUNOGLOBULIN HEAVY CHAIN AND/OR LIGHT CHAIN [00106] An antibody of the present disclosure contains two or more tags in the amino acid sequence of an Ig heavy chain constant region and/or an Ig light chain constant region. The tag is positioned between two amino acids in the constant region of a corresponding parent Ig heavy chain and/or Ig light chain, i.e., the Ig heavy chain or the Ig light chain without the tag in the constant region. In other words, the amino acid sequence of the tag may be present in an Ig heavy chain and/or an Ig light chain such that the tag amino acid sequence is directly flanked N-terminally by a first flanking sequence identical to a first contiguous sequence in a corresponding parent Ig heavy chain constant region and/or Ig light chain constant region, and C-terminally directly flanked by a second flanking sequence identical to a second contiguous sequence in the corresponding parent Ig heavy chain constant region or Ig light chain constant region. The first contiguous sequence is more N-terminal to the second contiguous sequence in the parent Ig heavy chain constant region and/or Ig light chain constant chain amino acid sequence. The first and second contiguous sequences are contiguous in the parent Ig heavy chain constant region and/or Ig light chain constant region. [00107] In some cases, a parent Ig heavy chain constant region has the sequence of SEQ ID NO: 91 or a sequence having at least 80%, for example, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity to the sequence of SEQ ID NO: 91. SEQ ID NO: 91 is provided below: [00108] ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLM ISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTP PVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK (SEQ ID NO: 91). Atty. Dkt: RDWD-048WO [00109] The tag sites in an Ig heavy chain constant region are referenced as CH1, 8V, 14S, 24A, 45A, 58Q, 60S, 61G, 91N, 94V, 116E, 186V, 284D, 288F, and CT. Each of these are described below. [00110] The tag “CH1” (SEQ ID NO: 1) is prepared by modifying the sequence “SGALTSGVH” (SEQ ID NO: 134) at amino acid positions 49 to 57 of SEQ ID NO: 91. The sequence “LTS” in SEQ ID NO: 134 is replaced with a sulfatase motif, i.e., X¹Z¹X²Z²X³Z³ as described elsewhere in this disclosure. These modifications produce the sequence of SGAX¹Z¹X²Z²X³Z³GVH (SEQ ID NO: 1) within an Ig heavy chain. An example of an Ig heavy chain comprising only the CH1 tag is provided in SEQ ID NO: 113. [00111] The tag “8V” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the valine residue at the 8^th position of SEQ ID NO: 91 to produce the sequence GPSX¹Z¹X²Z²X³Z³VFP (SEQ ID NO: 2) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 8V tag is provided in SEQ ID NO: 114. [00112] The tag “14S” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the serine residue at the 14^th position of SEQ ID NO: 91 to produce the sequence LAPX¹Z¹X²Z²X³Z³SSK (SEQ ID NO: 3) within an Ig heavy chain. An example of an Ig heavy chain comprising only a 14S tag is provided in SEQ ID NO: 115. [00113] The tag “24A” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the alanine residue at the 24^th position of SEQ ID NO: 91 to produce the sequence GTAX¹Z¹X²Z²X³Z³ALG (SEQ ID NO: 4) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 24A tag is provided in SEQ ID NO: 116. [00114] The tag “45A” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the alanine residue at the 45^th position of SEQ ID NO: 91 to produce the sequence NSGX¹Z¹X²Z²X³Z³ALT (SEQ ID NO: 5) within an Ig heavy chain. An example of an Ig heavy chain comprising only a 45A tag is provided in SEQ ID NO: 117. [00115] The tag “58Q” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the glutamine residue at the 58^th position of SEQ ID NO: 91 to produce the sequence AVLX¹Z¹X²Z²X³Z³QSS (SEQ ID NO: 6) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 58Q tag is provided in SEQ ID NO: 118. Atty. Dkt: RDWD-048WO [00116] The tag “60S” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the serine residue at the 60^th position of SEQ ID NO: 91 to produce the sequence LQSX¹Z¹X²Z²X³Z³SGL (SEQ ID NO: 7) within an Ig heavy chain. An example of an Ig heavy chain comprising only a 60S tag is provided in SEQ ID NO: 119. [00117] The tag “61G” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the glycine residue at the 61^st position of SEQ ID NO: 91 to produce the sequence QSSX¹Z¹X²Z²X³Z³GLY (SEQ ID NO: 8) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 61G tag is provided in SEQ ID NO: 120. [00118] The tag “91N” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the asparagine residue at the 91^st position of SEQ ID NO: 91 to produce the sequence KPSX¹Z¹X²Z²X³Z³NTK (SEQ ID NO: 9) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 91N tag is provided in SEQ ID NO: 121. [00119] The tag “94V” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the valine residue at the 94^th position of SEQ ID NO: 91 to produce the sequence NTKX¹Z¹X²Z²X³Z³VDK (SEQ ID NO: 10) within an Ig heavy chain. An example of an Ig heavy chain comprising only a 94V tag is provided in SEQ ID NO: 122. [00120] The tag “116E” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the glutamate residue at the 116^th position of SEQ ID NO: 91 to produce the sequence PAPX¹Z¹X²Z²X³Z³ELL (SEQ ID NO: 11) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 116E tag is provided in SEQ ID NO: 123. [00121] The tag “186V” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the valine residue at the 186^th position of SEQ ID NO: 91 to produce the sequence YRVX¹Z¹X²Z²X³Z³VSV (SEQ ID NO: 12) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 186V tag is provided in SEQ ID NO: 124. [00122] The tag “284D” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the aspartate residue at the 284^th position of SEQ ID NO: 91 to produce the sequence LDSX¹Z¹X²Z²X³Z³DGS (SEQ ID NO: 13) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 284D tag is provided in SEQ ID NO: 125. [00123] The tag “288F” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ before the phenylalanine residue at the 288^th position of SEQ ID NO: 91 to produce the sequence Atty. Dkt: RDWD-048WO GSFX¹Z¹X²Z²X³Z³FLY (SEQ ID NO: 14) within an Ig heavy chain. An example of an Ig heavy chain comprising only the 288F tag is provided in SEQ ID NO: 126. [00124] The tag “CT” is prepared by replacing the K at the C terminus of SEQ ID NO: 91 with the sequence SX¹Z¹X²Z²X³Z³GS. Thus, essentially, the subsequence “SPGK” (SEQ ID NO: 92) at the C-terminus of SEQ ID NO: 91 is replaced with the sequence SPGSX¹Z¹X²Z²X³Z³GS (SEQ ID NO: 15) within an Ig heavy chain. An example of an Ig heavy chain comprising only the CT tag is provided in SEQ ID NO: 127. [00125] Thus, an Ig heavy chain having the tags 58Q and 116E comprises the sequences of SEQ ID NO: 6 and SEQ ID NO: 11. An Ig heavy chain having the tags 58Q and 116E can have the sequence of SEQ ID NO: 99. Similarly, an Ig heavy chain having the tags 91N and 116E comprises the sequences of SEQ ID NO: 9 and SEQ ID NO: 11. An Ig heavy chain having the tags 91N and 116E can have the sequence of SEQ ID NO: 102. [00126] In some cases, an Ig heavy chain having any two tags as described herein shares at least 80%, for example, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity to the sequence of SEQ ID NO: 91 excluding the tag sequences. In other words, when the tag sequences are removed from an Ig heavy chain having any two tags as described herein, the resulting sequence is at least 80%, for example, at least 85%, at least 90%, at least 95%, or at least 99% identical to the sequence of SEQ ID NO: 91. [00127] In some cases, a parent Ig light chain constant region has the sequence of SEQ ID NO: 93 or a sequence having at least 80%, for example, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity to the sequence of SEQ ID NO: 93. SEQ ID NO: 93 is provided below: [00128] RTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQD SKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC (SEQ ID NO: 93). [00129] The tag sites in an Ig light chain constant region are referenced as 3.1, 5.1, 22A, 51S, and 5P. Each of these are described below. [00130] The tag “3.1” (SEQ ID NO: 16) is prepared by modifying the sequence “DNALQSG” (SEQ ID NO: 94) at amino acid positions 44 to 50 of SEQ ID NO: 93. The leucine in SEQ ID NO: 94 can be replaced with a sulfatase motif, i.e., X¹Z¹X²Z²X³Z³ thereby producing the Atty. Dkt: RDWD-048WO sequence of DNAX¹Z¹X²Z²X³Z³QSG (SEQ ID NO: 16) within an Ig light chain. An Ig light chain having only the 3.1 tag can have the sequence of SEQ ID NO: 128. [00131] The tag “5.1” (SEQ ID NO: 17) is prepared by modifying the sequence “HQGLSSPV” (SEQ ID NO: 133) at amino acid positions 91 to 98 of SEQ ID NO: 93. The sequence “LS” in SEQ ID NO: 133 is replaced with a sulfatase motif, X¹Z¹X²Z²X³Z³ thereby producing the sequence of HQGX¹Z¹X²Z²X³Z³SPV (SEQ ID NO: 17) within an Ig light chain. An Ig light chain having only the 5.1 tag can have the sequence of SEQ ID NO: 129. [00132] The tag “22A” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ after the alanine residue at the 23^rd position of SEQ ID NO: 93 to produce the sequence GTAX¹Z¹X²Z²X³Z³SVV (SEQ ID NO: 18) within an Ig light chain. An Ig light chain having only the 22A tag can have the sequence of SEQ ID NO: 130. [00133] The tag “51S” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ after the serine residue at the 52^nd position of SEQ ID NO: 93 to produce the sequence GNSX¹Z¹X²Z²X³Z³QES (SEQ ID NO: 19) within an Ig light chain. An Ig light chain having only the 51S tag can have the sequence of SEQ ID NO: 131. [00134] The tag “5P” is prepared by inserting the sequence X¹Z¹X²Z²X³Z³ after the proline residue at the 6^th position of SEQ ID NO: 93 to produce the sequence AAPX¹Z¹X²Z²X³Z³SVF (SEQ ID NO: 20) within an Ig light chain. An Ig light chain having only the 5P tag can have the sequence of SEQ ID NO: 132. [00135] Thus, an Ig light chain having the tag 3.1 comprises the sequences of SEQ ID NO: 16. An Ig light having the tag 3.1 can have the sequence of SEQ ID NO: 128. Similarly, an Ig light chain having the tag 5.1 comprises the sequences of SEQ ID NO: 17. An Ig light having the tag 5.1 can have the sequence of SEQ ID NO: 129. [00136] In some cases, an Ig light chain having a tag as described herein shares at least 80%, for example, at least 85%, at least 90%, at least 95%, or at least 99% sequence identity to the sequence of SEQ ID NO: 93 excluding the tag sequence. In other words, when the tag sequence is removed from an Ig light chain having any tag as described herein, the resulting sequence is at least 80%, for example, at least 85%, at least 90%, at least 95%, or at least 99% identical to the sequence of SEQ ID NO: 93. Atty. Dkt: RDWD-048WO [00137] In some aspects, an antibody disclosed herein comprises two or three tags in the heavy chain and/or the light chain of the antibody. [00138] Accordingly, in some embodiments, the disclosure provides an antibody comprising an Ig heavy chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence and the second amino acid sequence are selected from: SEQ ID NOs: 1 to 15. Thus, in such embodiments, an antibody comprises an Ig heavy chain comprising two tags as described herein. [00139] In some cases, the first amino acid sequence and the second amino acid second sequence, respectively, comprise: [00140] SEQ ID NO: 6 and SEQ ID NO: 11; [00141] SEQ ID NO:15 and SEQ ID NO: 11; [00142] SEQ ID NO: 15 and SEQ ID NO: 1; [00143] SEQ ID NO: 9 and SEQ ID NO: 11; [00144] SEQ ID NO: 15 and SEQ ID NO: 9; [00145] SEQ ID NO: 15 and SEQ ID NO: 6; [00146] SEQ ID NO: 8 and SEQ ID NO: 11; [00147] SEQ ID NO: 8 and SEQ ID NO: 15; [00148] SEQ ID NO: 3 and SEQ ID NO: 11; [00149] SEQ ID NO: 3 and SEQ ID NO: 6; [00150] SEQ ID NO: 15 and SEQ ID NO: 5; [00151] SEQ ID NO: 5 and SEQ ID NO: 11; [00152] SEQ ID NO: 5 and SEQ ID NO: 9; or [00153] SEQ ID NO: 12 and SEQ ID NO: 11. [00154] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 6 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 99. [00155] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, which is at least 90%, e.g., Atty. Dkt: RDWD-048WO at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 99. [00156] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 100. [00157] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 100. [00158] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 1. An example of such antibody has the sequence of SEQ ID NO: 101. [00159] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 101. [00160] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 9 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 102. [00161] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 102. [00162] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 9. An example of such antibody has the sequence of SEQ ID NO: 103. [00163] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 103. Atty. Dkt: RDWD-048WO [00164] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 6. An example of such antibody has the sequence of SEQ ID NO: 104. [00165] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 104. [00166] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 8 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 105. [00167] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 105. [00168] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 8 and the second amino acid sequence is SEQ ID NO: 15. An example of such antibody has the sequence of SEQ ID NO: 106. [00169] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 106. [00170] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 3 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 107. [00171] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 107. [00172] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the Atty. Dkt: RDWD-048WO first amino acid sequence is SEQ ID NO: 3 and the second amino acid sequence is SEQ ID NO: 6. An example of such antibody has the sequence of SEQ ID NO: 108. [00173] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 108. [00174] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 5. An example of such antibody has the sequence of SEQ ID NO: 109. [00175] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 109. [00176] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 5 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 110. [00177] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 110. [00178] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 5 and the second amino acid sequence is SEQ ID NO: 9. An example of such antibody has the sequence of SEQ ID NO: 111. [00179] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 111. [00180] In one embodiment, the disclosure provides an antibody comprising an Ig heavy chain comprising a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 12 and the second amino acid sequence is SEQ ID NO: 11. An example of such antibody has the sequence of SEQ ID NO: 112. Atty. Dkt: RDWD-048WO [00181] In certain embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 112. [00182] In some aspects, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is selected from SEQ ID NOs: 1 to 15 and the second amino acid sequence is selected from SEQ ID NOs: 16 to 20. Thus, in such embodiments, an antibody comprises an Ig heavy chain comprising a tag and an Ig light chain comprising a tag. [00183] In some cases, the first amino acid sequence and the second amino acid sequence, respectively, comprise: [00184] SEQ ID NO: 7 and SEQ ID NO: 18; [00185] SEQ ID NO: 12 and SEQ ID NO: 18; [00186] SEQ ID NO: 8 and SEQ ID NO: 18; [00187] SEQ ID NO: 11 and SEQ ID NO: 18; [00188] SEQ ID NO: 15 and SEQ ID NO: 19; [00189] SEQ ID NO: 10 and SEQ ID NO: 18; [00190] SEQ ID NO: 1 and SEQ ID NO: 18; [00191] SEQ ID NO: 5 and SEQ ID NO: 18; [00192] SEQ ID NO: 4 and SEQ ID NO: 18; [00193] SEQ ID NO: 1 and SEQ ID NO: 19; [00194] SEQ ID NO: 11 and SEQ ID NO: 19; [00195] SEQ ID NO: 5 and SEQ ID NO: 19; [00196] SEQ ID NO: 9 and SEQ ID NO: 18; [00197] SEQ ID NO: 8 and SEQ ID NO: 19; [00198] SEQ ID NO: 15 and SEQ ID NO: 18; [00199] SEQ ID NO: 6 and SEQ ID NO: 18; [00200] SEQ ID NO: 6 and SEQ ID NO: 19; [00201] SEQ ID NO: 2 and SEQ ID NO: 18; [00202] SEQ ID NO: 12 and SEQ ID NO: 19; Atty. Dkt: RDWD-048WO [00203] SEQ ID NO: 4 and SEQ ID NO: 19; [00204] SEQ ID NO: 7 and SEQ ID NO: 19; [00205] SEQ ID NO: 10 and SEQ ID NO: 19; [00206] SEQ ID NO: 4 and SEQ ID NO: 20; [00207] SEQ ID NO: 5 and SEQ ID NO: 20; [00208] SEQ ID NO: 8 and SEQ ID NO: 20; [00209] SEQ ID NO: 10 and SEQ ID NO: 20; [00210] SEQ ID NO: 2 and SEQ ID NO: 20; [00211] SEQ ID NO: 7 and SEQ ID NO: 20; [00212] SEQ ID NO: 12 and SEQ ID NO: 20; [00213] SEQ ID NO: 1 and SEQ ID NO: 20; or [00214] SEQ ID NO: 15 and SEQ ID NO: 20. [00215] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 7 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 119 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00216] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 119 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00217] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 12 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 124 and an Ig light chain comprising the sequence of SEQ ID NO: 130. Atty. Dkt: RDWD-048WO [00218] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 124 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00219] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 8 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 120 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00220] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 120 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00221] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 11 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 123 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00222] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 123 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. Atty. Dkt: RDWD-048WO [00223] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 127 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00224] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 127 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00225] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 10 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 122 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00226] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 122 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00227] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 1 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 113 and an Ig light chain comprising the sequence of SEQ ID NO: 130. Atty. Dkt: RDWD-048WO [00228] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 113 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00229] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 5 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 117 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00230] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 117 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00231] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 4 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 116 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00232] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 116 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. Atty. Dkt: RDWD-048WO [00233] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 1 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 113 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00234] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 113 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00235] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 11 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 123 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00236] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 123 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00237] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 5 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 117 and an Ig light chain comprising the sequence of SEQ ID NO: 131. Atty. Dkt: RDWD-048WO [00238] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 117 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00239] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 9 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 121 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00240] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 121 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00241] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 8 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 120 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00242] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 120 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. Atty. Dkt: RDWD-048WO [00243] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 127 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00244] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 127 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00245] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 6 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 118 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00246] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 118 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00247] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 6 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 118 and an Ig light chain comprising the sequence of SEQ ID NO: 131. Atty. Dkt: RDWD-048WO [00248] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 118 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00249] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 2 and the second amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 114 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00250] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 114 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00251] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 12 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 124 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00252] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 124 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. Atty. Dkt: RDWD-048WO [00253] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 4 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 116 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00254] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 116 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00255] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 7 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 119 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00256] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 119 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00257] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 10 and the second amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 122 and an Ig light chain comprising the sequence of SEQ ID NO: 131. Atty. Dkt: RDWD-048WO [00258] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 122 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00259] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 4 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 116 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00260] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 116 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00261] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 5 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 117 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00262] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 117 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. Atty. Dkt: RDWD-048WO [00263] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 8 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 120 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00264] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 120 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00265] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 10 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 122 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00266] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 122 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00267] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 2 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 114 and an Ig light chain comprising the sequence of SEQ ID NO: 132. Atty. Dkt: RDWD-048WO [00268] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 114 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00269] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 7 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 119 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00270] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 119 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00271] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 12 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 124 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00272] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 124 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. Atty. Dkt: RDWD-048WO [00273] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 1 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 113 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00274] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 113 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00275] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15 and the second amino acid sequence is SEQ ID NO: 20. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 127 and an Ig light chain comprising the sequence of SEQ ID NO: 132. [00276] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 127 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 132. [00277] A further aspect of the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence and the second amino acid sequence are selected from SEQ ID NOs: 1 to 15 and the third amino acid sequence is selected from SEQ ID Atty. Dkt: RDWD-048WO NOs: 16 to 20. Thus, in such embodiments, an antibody comprises an Ig heavy chain comprising two tags and an Ig light chain comprising a tag. [00278] In certain such embodiments, the first amino acid sequence, the second amino acid sequence, and the third amino acid sequence, respectively, comprise: [00279] SEQ ID NO: 9, SEQ ID NO: 11, and SEQ ID NO: 18; [00280] SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 18; [00281] SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 18; [00282] SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 18; [00283] SEQ ID NO: 8, SEQ ID NO: 11, and SEQ ID NO: 18; [00284] SEQ ID NO: 3, SEQ ID NO: 11, and SEQ ID NO: 18; [00285] SEQ ID NO: 3, SEQ ID NO: 6, and SEQ ID NO: 18; [00286] SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 16; [00287] SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 17; [00288] SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 16; [00289] SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 17; [00290] SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 19; [00291] SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 18; or [00292] SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 19. [00293] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 9, the second amino acid sequence is SEQ ID NO: 11, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 102 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00294] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 102 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least Atty. Dkt: RDWD-048WO 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00295] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 6, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 104 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00296] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 104 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00297] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 6, the second amino acid sequence is SEQ ID NO: 11, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 99 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00298] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 99 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00299] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid Atty. Dkt: RDWD-048WO sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 1, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 101 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00300] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 101 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00301] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 8, the second amino acid sequence is SEQ ID NO: 11, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 105 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00302] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 105 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00303] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 3, the second amino acid sequence is SEQ ID NO: 11, and the third amino acid sequence is SEQ ID NO: 18. An example of Atty. Dkt: RDWD-048WO such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 107 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00304] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 107 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00305] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 3, the second amino acid sequence is SEQ ID NO: 6, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 108 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00306] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 108 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00307] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 1, and the third amino acid sequence is SEQ ID NO: 16. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 101 and an Ig light chain comprising the sequence of SEQ ID NO: 128. [00308] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., Atty. Dkt: RDWD-048WO at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 101 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 128. [00309] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 1, and the third amino acid sequence is SEQ ID NO: 17. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 101 and an Ig light chain comprising the sequence of SEQ ID NO: 129. [00310] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 101 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 129. [00311] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 6, and the third amino acid sequence is SEQ ID NO: 16. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 104 and an Ig light chain comprising the sequence of SEQ ID NO: 128. [00312] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 104 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 128. Atty. Dkt: RDWD-048WO [00313] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 6, and the third amino acid sequence is SEQ ID NO: 17. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 104 and an Ig light chain comprising the sequence of SEQ ID NO: 129. [00314] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 104 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 129. [00315] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 15, the second amino acid sequence is SEQ ID NO: 1, and the third amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 101 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00316] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 101 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00317] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 6, the second amino acid Atty. Dkt: RDWD-048WO sequence is SEQ ID NO: 11, and the third amino acid sequence is SEQ ID NO: 18. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 99 and an Ig light chain comprising the sequence of SEQ ID NO: 130. [00318] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 99 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 130. [00319] In certain embodiments, the disclosure provides an antibody comprising an Ig heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence is SEQ ID NO: 6, the second amino acid sequence is SEQ ID NO: 11, and the third amino acid sequence is SEQ ID NO: 19. An example of such antibody has Ig heavy chain comprising the sequence of SEQ ID NO: 99 and an Ig light chain comprising the sequence of SEQ ID NO: 131. [00320] In certain such embodiments, an antibody of the present disclosure includes an Ig heavy chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 99 and an Ig light chain containing an amino acid sequence, excluding any tags, that is at least 90%, e.g., at least 95%, at least 97%, at least 99%, including 100% identical the sequence of SEQ ID NO: 131. [00321] In the one or more tags in the Ig heavy chain and/or the Ig light chain, in the subsequence X¹Z¹X²Z²X³Z³ within the tag: X¹ is present or absent, and when present, can be any amino acid; Z¹ is cysteine, serine, 2-formylglycine (fGly), or fGly’, wherein fGly’ is an fGly residue covalently bound to a payload; Z² is proline or alanine; Z³ is an aliphatic amino acid or a basic amino acid; X² and X³ are each independently any amino acid. Atty. Dkt: RDWD-048WO [00322] In a certain embodiment Z³ is arginine. [00323] In some cases, X¹ is present, which can be glycine, leucine, isoleucine, methionine, histidine, tyrosine, valine, serine, cysteine, or threonine. [00324] In some cases, wherein X² and X³ are each independently serine, threonine, alanine, valine, glycine, or cysteine. [00325] In certain embodiments, in the sequence of SEQ ID NO: 1 to 20, the subsequence X¹Z¹X²Z²X³Z³ can be LCTPSR (SEQ ID NO: 22) or LSTPSR (SEQ ID NO: 23), MCTPSR (SEQ ID NO: 24), VCTPSR (SEQ ID NO: 25), LCSPSR (SEQ ID NO: 26), LCAPSR (SEQ ID NO: 27), LCVPSR (SEQ ID NO: 28), LCGPSR (SEQ ID NO: 29), ICTPAR (SEQ ID NO: 30), LCTPSK (SEQ ID NO: 31), MCTPSK (SEQ ID NO: 32), VCTPSK (SEQ ID NO: 33), LCSPSK (SEQ ID NO: 34), LCAPSK (SEQ ID NO: 35), LCVPSK (SEQ ID NO: 36), LCGPSK (SEQ ID NO: 37), LCTPSA (SEQ ID NO: 38), ICTPAA (SEQ ID NO: 39), MCTPSA (SEQ ID NO: 40), VCTPSA (SEQ ID NO: 41), LCSPSA (SEQ ID NO: 42), LCAPSA (SEQ ID NO: 43), LCVPSA (SEQ ID NO: 44), LCGPSA (SEQ ID NO: 45), MSTPSR (SEQ ID NO: 46), VSTPSR (SEQ ID NO: 47), LSSPSR (SEQ ID NO: 48), LSAPSR (SEQ ID NO: 49), LSVPSR (SEQ ID NO: 50), LSGPSR (SEQ ID NO: 51), ISTPAR (SEQ ID NO: 52), LSTPSK (SEQ ID NO: 53), MSTPSK (SEQ ID NO: 54), VSTPSK (SEQ ID NO: 55), LSSPSK (SEQ ID NO: 56), LSAPSK (SEQ ID NO: 57), LSVPSK (SEQ ID NO: 58), LSGPSK (SEQ ID NO: 59), LSTPSA (SEQ ID NO: 60), ISTPAA (SEQ ID NO: 61), MSTPSA (SEQ ID NO: 62), VSTPSA (SEQ ID NO: 63), LSSPSA (SEQ ID NO: 64), LSAPSA (SEQ ID NO: 65), LSVPSA (SEQ ID NO: 66), and LSGPSA (SEQ ID NO: 67). [00326] In certain such cases, when the Z¹ residue of the subsequence X¹Z¹X²Z²X³Z³ is converted to fGly, it produces a sequence of M(fGly)TPSR (SEQ ID NO: 68), V(fGly)TPSR (SEQ ID NO: 69), L(fGly)SPSR (SEQ ID NO: 70), L(fGly)APSR (SEQ ID NO: 71), L(fGly)VPSR (SEQ ID NO: 72), L(fGly)GPSR (SEQ ID NO: 73), I(fGly)TPAR (SEQ ID NO: 74), L(fGly)TPSK (SEQ ID NO: 75), M(fGly)TPSK (SEQ ID NO: 76), V(fGly)TPSK (SEQ ID NO: 77), L(fGly)SPSK (SEQ ID NO: 78), L(fGly)APSK (SEQ ID NO: 79), L(fGly)VPSK (SEQ ID NO: 80), L(fGly)GPSK (SEQ ID NO: 81), L(fGly)TPSA (SEQ ID NO: 82), I(fGly)TPAA (SEQ ID NO: 83), M(fGly)TPSA (SEQ ID NO: 84), V(fGly)TPSA (SEQ ID NO: 85), L(fGly)SPSA (SEQ ID NO: 86), L(fGly)APSA (SEQ ID NO: 87), L(fGly)VPSA (SEQ ID NO: 88), L(fGly)GPSA (SEQ ID NO: 89), and L(fGly)TPSR (SEQ ID NO: 90). PARENT HEAVY AND/OR LIGHT CHAINS Atty. Dkt: RDWD-048WO [00327] The parent heavy chain and/or light chain can be from an Ig, such as IgG. Thus, in some cases, the Ig heavy chain is an IgG heavy chain and the Ig light chain is an IgG kappa light chain. [00328] The parent heavy chain can be an IgG1, IgG2, IgG3, or IgG4 heavy chain, having an Ig constant region amino acid sequence, e.g., as shown in SEQ ID NOs: 96 to 98. [00329] Thus, in some cases, the Ig heavy chain is a human Ig heavy chain, e.g., human IgG1, human IgG2, human IgG3, or human IgG4 heavy chain. In some cases, the Ig heavy chain constant region is a human Ig heavy chain constant region, e.g., human IgG1, human IgG2, human IgG3, or human IgG4 heavy chain constant region. In some cases, the parent IgG1 heavy chain, on which the present antibody may be based, includes a constant region amino acid sequence 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 91. In some cases, the parent IgG2 heavy chain, on which the present antibody may be based, includes a constant region amino acid sequence 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 96. In some cases, the parent IgG3 heavy chain, on which the present antibody may be based, includes a constant region amino acid sequence 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 97. In some cases, the parent IgG4 heavy chain, on which the present antibody may be based, includes a constant region amino acid sequence 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 98. [00330] Thus, in some embodiments, an antibody of the present disclosure, containing one or two tags, may include an Ig heavy chain derived from a parent Ig heavy chain that is based on an IgG1 heavy chain, where the antibody contains an IgG1 heavy chain that includes a constant region amino acid sequence, excluding any tags, that is 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 91. [00331] In some embodiments, an antibody of the present disclosure, containing a tag, may include an Ig heavy chain derived from a parent Ig heavy chain that is based on an IgG2 Atty. Dkt: RDWD-048WO heavy chain, where the antibody contains an IgG2 heavy chain that includes a constant region amino acid sequence, excluding any tags, that is 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 96. [00332] In some embodiments, an antibody of the present disclosure, containing a tag, may include an Ig heavy chain derived from a parent Ig heavy chain that is based on an IgG3 heavy chain, where the antibody contains an IgG3 heavy chain that includes a constant region amino acid sequence, excluding any tags, that is 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 97. [00333] In some embodiments, an antibody of the present disclosure, containing a tag, may include an Ig heavy chain derived from a parent Ig heavy chain that is based on an IgG4 heavy chain, where the antibody contains an IgG4 heavy chain that includes a constant region amino acid sequence, excluding any tags, that is 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 98. [00334] Sequence alignments between the sequence of IgG1 heavy chain with the sequence of IgG2, IgG3, or IgG4 heavy chain could be used to identify a tag location that corresponds to the tag locations described herein. For example, FIG.13 of U.S. Patent No. 11,466,096 shows such alignment, which could be used to identify appropriate tag site corresponding to a tag site described herein, noting that the amino acid position in the corresponding heavy chain may not be the same. In other words, the alanine residue corresponding to the 24A position of SEQ ID NO: 91 may not be the 24^th amino acid in the sequence of SEQ ID NO: 96, 97, or 98. [00335] The present disclosure contemplates an antibody that includes an Ig heavy chain based on any suitable allotype, e.g., human allotype. Certain such allotypes are described in the U.S. Patent No.11,466,096, and such embodiments are within the purview of the disclosure. [00336] A parent light chain may be an Ig kappa light chain, having an Ig constant region amino acid sequence, e.g., as shown in SEQ ID NO: 93. Thus, in some cases, the Ig light chain is Atty. Dkt: RDWD-048WO a human Ig light chain. In some cases, the Ig light chain constant region is a human Ig light chain constant region. In some cases, the parent Ig light chain includes a constant region amino acid sequence 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 93. Thus, an antibody of the present disclosure, containing a tag, may include an Ig light chain derived from a parent Ig light chain that is based on an Ig kappa light chain, where the antibody contains an Ig light chain that includes a constant region amino acid sequence, exclusive of any tags, that is 75% or more, e.g., 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, and up to 100% identical to the amino acid sequence set forth in SEQ ID NO: 93. [00337] The present disclosure contemplates an antibody that includes an Ig light chain based on any suitable allotype, e.g., human allotype, of Ig kappa light chain. Certain such allotypes are described in the U.S. Patent No.11,208,632, and such embodiments are within the purview of the disclosure. FGLY-MODIFIED ANTIBODIES [00338] A tagged antibody, as described above, may be modified, e.g., by oxidation of the side chain of a cysteine or serine residue in the tag into an aldehyde side chain, such that the tag is converted to a converted tag containing an fGly, as described above, to generate an fGly-modified antibody. Where the Ig heavy chain includes a tag containing an FGE substrate motif of formula I, as described above, Z¹ may be modified to fGly through the action of FGE, to generate a converted tag that includes an amino acid sequence of the formula X¹(fGly)X²Z²X³Z³, where X¹, X², X³, Z², and Z³ are as described above. [00339] The enzyme that oxidizes cysteine or serine in a sulfatase motif to fGly is referred to herein as an FGE. As discussed above, “FGE” is used herein to refer to fGly- generating enzymes that mediate conversion of a cysteine (C) of a sulfatase motif to fGly as well as fGly-generating enzymes that mediate conversion of serine (S) of a sulfatase motif to fGly. In general, the literature refers to fGly-generating enzymes that convert a C to fGly in a sulfatase motif as FGEs, and refers to enzymes that convert S to fGly in a sulfatase motif as Ats- B-like. However, for purposes of the present disclosure “FGE” is used generically to refer to Atty. Dkt: RDWD-048WO both types of fGly-generating enzymes, with the understanding that an appropriate FGE will be selected according to the target reactive partner containing the appropriate sulfatase motif (i.e., C-containing or S-containing). [00340] Certain details of the FGE used to facilitate conversion of cysteine or serine to fGly in a sulfatase motif of a tag of a target polypeptide are described in the U.S. Patent Nos. 11,466,096 and 11,208,632, which are incorporated by reference in their entireties. The use of such FGEs are within the purview of this disclosure. [00341] Moreover, any suitable method for generating a tagged antibody having a sulfatase motif in its Ig, e.g., Ig heavy chain and/or Ig light chain, and converting the tag to include an fGly residue, may be used, e.g., as described in US20120183566, which is incorporated herein by reference in its entirety. [00342] Thus, the present disclosure includes an fGly-modified antibody that includes converted tags in an fGly-modified Ig heavy chain and/or Ig light chain, where the converted tag contains an amino acid sequence of the formula: X¹(fGly)X²Z²X³Z³ (II) where fGly is a formylglycine residue; Z² is either a proline or alanine residue (which can also be represented by (P/A)); Z³ is a basic amino acid (e.g., arginine (R), and may be lysine (K) or histidine (H), usually lysine), or an aliphatic amino acid (alanine (A), glycine (G), leucine (L), valine (V), isoleucine (I), or proline (P), usually A, G, L, V, or I; X¹ is present or absent and, when present, can be any amino acid, though usually an aliphatic amino acid, a sulfur-containing amino acid, or a polar, uncharged amino acid, (i.e., other than an aromatic amino acid or a charged amino acid), usually L, M, V, S or T, more usually L, M, S or V; and X² and X³ independently can be any amino acid, though usually an aliphatic amino acid, a polar, uncharged amino acid, or a sulfur containing amino acid (i.e., other than an aromatic amino acid or a charged amino acid), usually S, T, A, V, G or C, more usually S, T, A, V or G. [00343] As the converted tag may be derived from an unconverted tag, e.g., through the oxidation of a cysteine or serine in the sulfatase motif of a tag via the action of FGE, the position of the converted tag may be defined by the position of the tag in the Ig heavy chain and/or the Ig light chain, as described above. Thus in some embodiments, an fGly-modified antibody of the present disclosure includes an fGly-modified Ig heavy chain and/or Ig light Atty. Dkt: RDWD-048WO chain that includes a converted tag having an amino acid sequence of the formula X¹Z¹X²Z²X³Z³, where X¹, X², X³, Z² and Z³ are as described above, and where Z¹ is fGly. ANTIBODY CONJUGATES [00344] An antibody containing fGly-modified Ig heavy chain and/or Ig light chain, as described above, may be modified to covalently attach a moiety of interest (i.e., a payload, e.g., drug) to the antibody in a site-specific manner, to produce an antibody conjugate. As described above, the aldehyde moiety of the fGly residue in the converted tag provides a bioorthogonal reactive side chain with which an aldehyde-reactive group attached to a payload, e.g., a drug functionalized with an aldehyde-reactive group, can react in a chemoselective manner to form a covalent bond between the payload (e.g., drug ) and the Ig heavy chain and/or the Ig light chain via the fGly residue, to form an antibody-payload conjugate. [00345] Thus, the present disclosure includes an antibody conjugate that includes a modified tag in an Ig heavy chain and/or an Ig light chain, where the modified tag contains an amino acid sequence of the formula: X¹(fGly’)X²Z²X³Z³ (III) where fGly’ is a formylglycine residue modified with a payload (e.g., drug) covalently attached thereto; Z² is either a proline or alanine residue (which can also be represented by (P/A)); Z³ is a basic amino acid (e.g., arginine (R), and may be lysine (K) or histidine (H), usually lysine), or an aliphatic amino acid (alanine (A), glycine (G), leucine (L), valine (V), isoleucine (I), or proline (P), usually A, G, L, V, or I; X¹ is present or absent and, when present, can be any amino acid, though usually an aliphatic amino acid, a sulfur-containing amino acid, or a polar, uncharged amino acid, (i.e., other than an aromatic amino acid or a charged amino acid), usually L, M, V, S or T, more usually L, M, S or V; and X² and X³ independently can be any amino acid, though usually an aliphatic amino acid, a polar, uncharged amino acid, or a sulfur containing amino acid (i.e., other than an aromatic amino acid or a charged amino acid), usually S, T, A, V, G or C, more usually S, T, A, V or G. [00346] As the modified tag, having a payload (e.g., drug) conjugated thereto, may be derived from a converted tag, e.g., through the reaction of an aldehyde-reactive reactive Atty. Dkt: RDWD-048WO partner containing the payload (e.g., drug with the aldehyde group of fGly, the position of the modified tag may be defined by the position of the converted tag in the Ig heavy chain, which in turn may be defined by the position of the tag in the Ig heavy chain and/or the light chain, as described above. Thus in some embodiments, an antibody conjugate of the present disclosure includes an Ig heavy chain and/or an Ig light chain conjugate that includes a modified tag having an amino acid sequence of the formula X¹Z¹X²Z²X³Z³, where X¹, X², X³, Z² and Z³ are as described above, and where Z¹ is fGly’, where fGly’ is a formylglycine residue modified with a payload (e.g., drug) covalently attached thereto. [00347] As described above, the antibody conjugate that includes a payload conjugated to the present antibody via an fGly of a converted tag in an Ig heavy chain and/or an Ig light chain may exhibit in solution a proportion of antibody monomers of about 20% or higher, e.g., 30% or higher, 40% or higher, 60% or higher, 80% or higher, including 90% or higher. [00348] The structure of fGly’ may vary, and may depend on the structure of the aldehyde-reactive group used to react a reactive partner containing the payload (e.g., drug) with the aldehyde side chain of the fGly residue in a converted tag of an fGly-modified antibody. fGly’ may include any suitable linkage between the Ig backbone and the payload (e.g., drug). [00349] In some cases, the payload (e.g., drug) is covalently bound to the converted tag through the fGly, which is modified, through its reaction with the aldehyde-reactive group, to form a hydrazone, oxime, semicarbazone (e.g., thiosemicarbozone), alkyl, alkenyl, acyloxy, hydrazinyl-indolyl, hydrazinyl-imidazoyl, hydrazinyl-pyrrolyl, hydrazinyl-furanyl or a pyrazalinone linkage, or derivatives of such linkages, with the payload (e.g., drug). A hydrazinyl-indolyl linkage may include, e.g., a partially unsaturated pyrazole or pyridazine ring, or a partially unsaturated pyridazine or 1,2-diazepine ring. A pyrazalinone-derived linkage may include a cyclic linkage derived from a pyrazalinone. In some cases, a hydrazinyl-substituted heteroaryl ring-derived linkage includes a cyclic linkage derived from, e.g., a hydrazinyl- substituted 5-membered heteroaryl ring compound, where one or more atoms in the ring is a heteroatom (e.g., N, O or S). The hydrazinyl-substituted heteroaryl ring-derived linkage may include a hydrazinyl-imidazoyl, hydrazinyl-pyrrolyl, or a hydrazinyl-furanyl linkage. Suitable linkages between the fGly of a converted tag and the payload are described in, e.g., Atty. Dkt: RDWD-048WO US20120183566, US20140141025, and WO2014074218, each of which is incorporated herein by reference. [00350] The payload (e.g., drug), in some cases, may be covalently bound to the fGly of a converted tag via one or more linking groups, in addition to the covalent linkage formed by a reaction between the aldehyde-reactive group and the aldehyde group of fGly of the converted tag. Thus the linking group may serve as a spacer between the payload (e.g., drug) and the covalent linkage with the modified fGly of the tag in the Ig heavy chain conjugate. The linking group may be any suitable linking group. In some cases, the linking group includes polyethylene glycol (PEG); amino acids; alkyl groups, including substituted alkyl groups; a protease cleavable group; esters; acyloxy groups, including substituted acyloxy groups, etc. In some cases, the linking group is a branched hydrazino-iso-pictet-spengler (HIPS) or a tandem- cleavage linker. Additional linking groups are described in, e.g., US20150157736, which is incorporated by reference herein. In some embodiments, the linking group includes a 4- aminopiperidine (4AP) derivative. [00351] In some cases, two or more payloads are conjugated to an antibody. For example, a linker, such as a HIPS functionalized linker is conjugated to two or more payloads, which is then conjugated to aldehyde tags on an antibody. Thus, two or more payloads can be conjugated to each aldehyde tag. [00352] In some cases, in addition to one or more payloads conjugated to tags described herein, an antibody can further comprise an additional payload conjugated to cysteine residues involved in interchain disulfide bonds. Such additional payloads can be conjugated to cysteine residues involved in interchain disulfide bonds via a different linker than the covalent conjugation between the one or more payloads and the fGly’ of the tags described herein. P^ARENT A^NTIBODIES [00353] An antibody conjugate of the present disclosure can include: 1) an Ig heavy chain constant region conjugated to a payload (e.g., drug) of interest; and an Ig light chain constant region that is not conjugated to a payload (e.g., drug); or 2) an Ig heavy chain constant region conjugated to a payload (e.g., drug); and an Ig light chain constant region conjugated to a payload (e.g., drug). In some cases, an antibody comprises an Ig heavy chain has two tags, Atty. Dkt: RDWD-048WO each conjugated to a payload. In some cases, an antibody comprises an Ig heavy chain having one tag conjugated to a payload and an Ig light chain having one tag conjugated to a payload. In some cases, an antibody comprises an Ig heavy chain having two tags, each conjugated to a payload and an Ig light chain having one tag conjugated to a payload. [00354] An antibody can also include V_H and/or V_L domains. [00355] An antibody conjugate can have any of a variety of antigen-binding specificities, including, e.g., an antigen present on a cancer cell; an antigen present on an autoimmune cell; an antigen present on a pathogenic microorganism; an antigen present on a virus-infected cell (e.g., a human immunodeficiency virus-infected cell), e.g., CD4 or gp120; an antigen present on a diseased cell; and the like. For example, an antibody conjugate can bind an antigen, where the antigen is present on the surface of the cell. The binding specificity, affinity, etc., of the antibody conjugate may be determined by at least the light and heavy chain variable region CDR sequences and/or the light and heavy chain variable regions (including the framework regions) included in the antibody conjugate. Thus the binding specificity, affinity, etc., of the antibody conjugate typically may have substantially the same antigen binding specificity, affinity, etc., as an antibody that may not be conjugated to a payload, or be tagged, and which has at least the same light and heavy chain variable region CDR sequences and/or the same light and heavy chain variable regions as the antibody conjugate. [00356] An antibody conjugate of the present disclosure can bind antigen with a suitable binding affinity, e.g., from about 5 x 10^-6 M to about 10^-7 M, from about 10^-7 M to about 5 x 10- ⁷ M, from about 5 x 10^-7 M to about 10^-8 M, from about 10^-8 M to about 5 x 10^-8 M, from about 5 x 10^-8 M to about 10^-9 M, or a binding affinity greater than 10^-9 M (i.e., KD less than 10^-9 M). [00357] As non-limiting examples, a subject antibody conjugate can bind an antigen present on a cancer cell (e.g., a tumor-specific antigen; an antigen that is over-expressed on a cancer cell; etc.), and the attached payload can be a cytotoxic compound (e.g., a cytotoxic small molecule, a cytotoxic synthetic peptide, etc.). For example, a subject antibody conjugate can be specific for CD19, where the attached payload is a cytotoxic compound (e.g., a cytotoxic small molecule, a cytotoxic synthetic peptide, etc.). As another example, a subject antibody conjugate can be specific for CD22, where the attached payload can be a cytotoxic compound (e.g., a cytotoxic small molecule, a cytotoxic synthetic peptide, etc.). Alternatively, a subject Atty. Dkt: RDWD-048WO antibody conjugate can be specific for CD79b, where the attached payload can be a cytotoxic compound (e.g., a cytotoxic small molecule, a cytotoxic synthetic peptide, etc.). Alternatively, a subject antibody conjugate can be specific for CD33, where the attached payload can be a cytotoxic compound (e.g., a cytotoxic small molecule, a cytotoxic synthetic peptide, etc.). [00358] Additional examples of tumor-specific antigens include HER2, CD30, CD56, CD66/CEACAM5, CD70, CD74, CD138, Nectin-4, Mesothelin, Transmembrane glycoprotein NMB (GPNMB), Prostate-Specific Membrane Antigen (PSMA), SLC44A4, CA6, and CA-IX. [00359] In certain embodiments, the antibody is derived from an antibody selected from Trastuzumab, Polatuzumab, Gemtuzumab, anti-NaPi2b antibody, and anti-SGN-33a antibody. Further examples of tumor specific antigens are known in the art and antibodies specific to such antigens are within the purview of the disclosure. [00360] As further non-limiting examples, a subject antibody conjugate can bind an antigen present on a cell infected with a virus (e.g., where the antigen is encoded by the virus; where the antigen is expressed on a cell type that is infected by a virus; etc.), and the payload can be a viral fusion inhibitor. For example, a subject antibody conjugate can bind CD4, and the attached payload can be a viral fusion inhibitor. As another example, a subject antibody conjugate can bind gp120, and the attached payload can be a viral fusion inhibitor. [00361] In some cases, a subject antibody conjugate can bind an antigen present in a bacterial or a fungal cells, such as antigens present in a bacterial or fungal cell surface. Certain such antigens include bacterial or fungal toxins, cell-surface polysaccharides, cell-surface lipids, cell-surface proteins. Certain such examples are described by Motley et al. (2019), Curr Opin Infect Dis.; 32(3): 210–216, which is incorporated herein by reference in its entirety. Additional examples of bacterial or fungal specific antigens are known in the art and antibodies against such antigens are within the purview of the disclosure. P^AYLOADS [00362] A payload conjugated to an antibody of the present disclosure includes any suitable moiety (e.g., a small molecule drug, a detectable label, a water-soluble polymer, a synthetic peptide, a protein degrader, an oligonucleotide, a radiolabeled ligand, an antimicrobial, etc.) that, prior to conjugation to an fGly-modified antibody, can be Atty. Dkt: RDWD-048WO functionalized to from an aldehyde-reactive reactive partner that includes an aldehyde- reactive group attached to the payload. [00363] In some cases, the payload is a small molecule drug. The small molecule drug can be an immunomodulator, a cytotoxic molecule, or a cancer chemotherapeutic agent. A cancer chemotherapeutic agent can be an alkylating agent, a microtubule inhibitor, topoisomerase inhibitor, kinase inhibitor, a nitrosourea, an antimetabolite, an antitumor antibiotic, a vinca alkaloid, or a steroid hormone. [00364] The payload can also be a water-soluble polymer, such as poly(ethylene glycol). [00365] The payload can be a detectable label, such as an imaging agent or a radiolabeled ligand. In some cases, the payload is an antimicrobial agent, such as an antiviral, particularly, a viral fusion inhibitor, an antibacterial, or an antifungal. [00366] A payload includes any of a variety of compounds, as described above, e.g., a drug (e.g., a peptide drug, a small molecule drug, and the like), a water-soluble polymer, a detectable label, a synthetic peptide, etc. In general, the payload or payloads (e.g., drug or drugs) can provide for one or more of a wide variety of functions or features. Moieties of interest include, without limitation, detectable labels (e.g., dye labels (e.g., chromophores, fluorophores), biophysical probes (spin labels, nuclear magnetic resonance (NMR) probes), Förster Resonance Energy Transfer (FRET)-type labels (e.g., at least one member of a FRET pair, including at least one member of a fluorophore/quencher pair), Bioluminescence Resonance Energy Transfer (BRET)-type labels (e.g., at least one member of a BRET pair), immunodetectable tags (e.g., FLAG (e.g., DYKDDDDK (SEQ ID NO: 136)), His(6), and the like), localization tags (e.g., to identify association of a tagged polypeptide at the tissue or molecular cell level (e.g., association with a tissue type, or particular cell membrane)), and the like); light- activated dynamic moieties (e.g., azobenzene mediated pore closing, azobenzene mediated structural changes, photodecaging recognition motifs); water soluble polymers (e.g., PEGylation); purification tags (e.g., to facilitate isolation by affinity chromatography (e.g., attachment of a FLAG epitope, e.g., DYKDDDDK (SEQ ID NO: 136)); membrane localization domains (e.g., lipids or glycophosphatidylinositol (GPI)-type anchors); immobilization tags (e.g., to facilitate attachment of the polypeptide to a surface, including selective attachment); drugs (e.g., to facilitate drug targeting, e.g., through attachment of the drug to an antibody); toxins; Atty. Dkt: RDWD-048WO targeted delivery moieties, (e.g., ligands for binding to a target receptor (e.g., to facilitate viral attachment, attachment of a targeting protein present on a liposome, etc.)), other molecules for delivery to the cell and which can provide for a pharmacological activity or can serve as a target for delivery of other molecules, and the like. [00367] Also contemplated is a covalently attached payload (e.g., drug) that comprises one of a pair of binding partners (e.g., a ligand, a ligand-binding portion of a receptor, a receptor-binding portion of a ligand, etc.). For example, the payload can comprise a polypeptide that serves as a viral receptor and, upon binding with a viral envelope protein or viral capsid protein, facilitates attachment of virus to the cell surface with which the antibody conjugate is associated, e.g., is bound. Alternatively, the payload comprises an antigen that is specifically bound by an antibody (e.g., monoclonal antibody), to facilitate detection and/or separation of host cells bound to the antibody conjugate containing the payload. Water-soluble polymers [00368] In some cases, an antibody conjugate comprises a covalently linked payload that is a water-soluble polymer. A moiety of particular interest is a water-soluble polymer. A "water-soluble polymer" refers to a polymer that is soluble in water and is usually substantially non-immunogenic, and usually has an atomic molecular weight greater than about 1,000 Daltons. The methods and compositions described herein can be used to attach one or more water-soluble polymers to a tagged and converted polypeptide. Attachment of a water-soluble polymer (e.g., PEG) of a polypeptide, particularly a pharmaceutically active (therapeutic) polypeptide can be desirable as such modification can increase therapeutic index by increasing serum half-life as a result of increased proteolytic stability and/or decreased renal clearance. Additionally, attachment of one or more polymers (e.g., PEGylation) can reduce immunogenicity of protein pharmaceuticals. [00369] In some embodiments, the water-soluble polymer has an effective hydrodynamic molecular weight of greater than about 10,000 Da, greater than about 20,000 to 500,000 Da, greater than about 40,000 Da to 300,000 Da, greater than about 50,000 Da to 70,000 Da, usually greater than about 60,000 Da. In some embodiments, the water-soluble polymer has an effective hydrodynamic molecular weight of from about 10 kDa to about 20 kDa, from about 20 kDa to about 25 kDa, from about 25 kDa to about 30 kDa, from about 30 Atty. Dkt: RDWD-048WO kDa to about 50 kDa, or from about 50 kDa to about 100 kDa. By "effective hydrodynamic molecular weight" is intended the effective water-solvated size of a polymer chain as determined by aqueous-based size exclusion chromatography (SEC). When the water-soluble polymer contains polymer chains having polyalkylene oxide repeat units, such as ethylene oxide repeat units, each chain can have an atomic molecular weight of between about 200 Da and about 80,000 Da, or between about 1,500 Da and about 42,000 Da, with 2,000 to about 20,000 Da being of particular interest. Unless referred to specifically, molecular weight is intended to refer to atomic molecular weight. Linear, branched, and terminally charged water soluble polymers (e.g., PEG) are of particular interest. [00370] Polymers useful as moieties to be conjugated to an fGly-modified antibody to form an antibody conjugate can have a wide range of molecular weights, and polymer subunits. These subunits may include a biological polymer, a synthetic polymer, or a combination thereof. Examples of such water-soluble polymers include: dextran and dextran derivatives, including dextran sulfate, P-amino cross linked dextrin, and carboxymethyl dextrin, cellulose and cellulose derivatives, including methylcellulose and carboxymethyl cellulose, starch and dextrines, and derivatives and hydroylactes of starch, polyalklyene glycol and derivatives thereof, including polyethylene glycol, methoxypolyethylene glycol, polyethylene glycol homopolymers, polypropylene glycol homopolymers, copolymers of ethylene glycol with propylene glycol, wherein said homopolymers and copolymers are unsubstituted or substituted at one end with an alkyl group, heparin and fragments of heparin, polyvinyl alcohol and polyvinyl ethyl ethers, polyvinylpyrrolidone, aspartamide, and polyoxyethylated polyols, with the dextran and dextran derivatives, dextrine and dextrine derivatives. It will be appreciated that various derivatives of the specifically recited water-soluble polymers are also contemplated. [00371] Water-soluble polymers such as those described above are well known, particularly the polyalkylene oxide based polymers such as polyethylene glycol "PEG". Suitable polymers include, without limitation, those containing a polyalkylene oxide, polyamide alkylene oxide, or derivatives thereof, including polyalkylene oxide and polyamide alkylene oxide comprising an ethylene oxide repeat unit of the formula -(CH₂-CH₂-O)-. Further exemplary polymers of interest include a polyamide having a molecular weight greater than Atty. Dkt: RDWD-048WO about 1,000 Daltons of the formula -[C(O)-X-C(O)-NH-Y-NH]n- or -[NH-Y-NH-C(O)-X-C(O)]_n-, where X and Y are divalent radicals that may be the same or different and may be branched or linear, and n is a discrete integer from 2-100, usually from 2 to 50, and where either or both of X and Y comprises a biocompatible, substantially non-antigenic water-soluble repeat unit that may be linear or branched. Further exemplary water-soluble repeat units comprise an ethylene oxide of the formula -(CH₂-CH₂-O)- or -(CH₂-CH₂-O)- . The number of such water-soluble repeat units can vary significantly, with the usual number of such units being from 2 to 500, 2 to 400, 2 to 300, 2 to 200, 2 to 100, and most usually 2 to 50. An exemplary embodiment is one in which one or both of X and Y is selected from: -((CH2) n1-(CH2-CH2-O)n2-(CH2)- or -((CH2)n1-(O- CH2-CH2)n2-(CH2) n- 1-), where n1 is 1 to 6, 1 to 5, 1 to 4 and most usually 1 to 3, and where n2 is 2 to 50, 2 to 25, 2 to 15, 2 to 10, 2 to 8, and most usually 2 to 5. A further exemplary embodiment is one in which X is -(CH2-CH2)-, and where Y is -(CH2-(CH2-CH2-O)3-CH2-CH2-CH2)- or -(CH2-CH2-CH2-(O-CH2-CH2)3-CH2)-. [00372] The polymer can include one or more spacers or linkers. Exemplary spacers or linkers include linear or branched moieties comprising one or more repeat units employed in a water-soluble polymer, diamino and or diacid units, natural or unnatural amino acids or derivatives thereof, as well as aliphatic moieties, including alkyl, aryl, heteroalkyl, heteroaryl, alkoxy, and the like, which can contain, for example, up to 18 carbon atoms or even an additional polymer chain. [00373] The polymer moiety, or one or more of the spacers or linkers of the polymer moiety when present, may include polymer chains or units that are biostable or biodegradable. For example, polymers with repeat linkages have varying degrees of stability under physiological conditions depending on bond lability. Polymers with such bonds can be categorized by their relative rates of hydrolysis under physiological conditions based on known hydrolysis rates of low molecular weight analogs, e.g., from less stable to more stable, e.g., polyurethanes (-NH-C(O)-O-) > polyorthoesters (-O-C((OR)(R'))-O-) > polyamides (-C(O)-NH-). Similarly, the linkage systems attaching a water-soluble polymer to a target molecule may be biostable or biodegradable, e.g., from less stable to more stable: carbonate (-O-C(O)-O-)>ester (-C(O)-O-) > urethane (-NH-C(O)-O-) > orthoester (-O-C((OR)(R'))-O-) > amide (-C(O)-NH-). In general, it may be desirable to avoid use of sulfated polysaccharide, depending on the lability Atty. Dkt: RDWD-048WO of the sulfate group. In addition, it may be less desirable to use polycarbonates and polyesters. These bonds are provided by way of example, and are not intended to limit the types of bonds employable in the polymer chains or linkage systems of the water-soluble polymers useful in the modified aldehyde tagged polypeptides disclosed herein. Synthetic peptides [00374] In some cases, an antibody conjugate comprises a covalently linked peptide, e.g., a peptide covalently linked to fGly of a converted tag of an Ig heavy chain of an antibody. Suitable peptides include, but are not limited to, cytotoxic peptides; angiogenic peptides; anti- angiogenic peptides; peptides that activate B cells; peptides that activate T cells; anti-viral peptides; peptides that inhibit viral fusion; peptides that increase production of one or more lymphocyte populations; anti-microbial peptides; growth factors; growth hormone-releasing factors; vasoactive peptides; anti-inflammatory peptides; peptides that regulate glucose metabolism; an anti-thrombotic peptide; an anti-nociceptive peptide; a vasodilator peptide; a platelet aggregation inhibitor; an analgesic; and the like. [00375] Where the covalently attached moiety is a peptide, the peptide can be chemically synthesized to include a group reactive with a converted fGly-containing Ig. A suitable synthetic peptide has a length of from about 5 amino acids to about 100 amino acids, or longer than 100 amino acids; e.g., a suitable peptide has a length of from about 5 amino acids (aa) to about 10 aa, from about 10 aa to about 15 aa, from about 15 aa to about 20 aa, from about 20 aa to about 25 aa, from about 25 aa to about 30 aa, from about 30 aa to about 40 aa, from about 40 aa to about 50 aa, from about 50 aa to about 60 aa, from about 60 aa to about 70 aa, from about 70 aa to about 80 aa, from about 80 aa to about 90 aa, or from about 90 aa to about 100 aa. [00376] A peptide can be modified to contain an α-nucleophile-containing moiety (e.g., an aminooxy or hydrazide moiety), e.g., can be reacted with the fGly-containing Ig to yield a conjugate in which the aldehyde-tagged Ig and peptide are linked by a hydrazone or oxime bond, respectively. Exemplary methods of synthesizing a peptide, such that the synthetic peptide comprising a reactive group reactive with a converted aldehyde tag, are described above. Atty. Dkt: RDWD-048WO [00377] Suitable peptides include, but are not limited to, hLF-11 (an 11-amino acid N- terminal fragment of lactoferrin), an anti-microbial peptide; granulysin, an anti-microbial peptide; Plectasin (NZ2114; SAR 215500), an anti-microbial peptide; viral fusion inhibitors such as Fuzeon (enfuvirtide), TRI-1249 (T-1249; see, e.g., Matos et al. (2010) PLoS One 5:e9830), TRI- 2635 (T-2635; see, e.g., Eggink et al. (2009) J. Biol. Chem.284:26941), T651, and TRI-1144; C5a receptor inhibitors such as PMX-53, JPE-1375, and JSM-7717; POT-4, a human complement factor C3 inhibitor; Pancreate (an INGAP derivative sequence, a HIP-human proislet protein); somatostatin; a somatostatin analog such as DEBIO 8609 (Sanvar), octreotide, octreotide (C2L), octreotide QLT, octreotide LAR, Sandostatin LAR, SomaLAR, Somatuline (lanreotide), see, e.g., Deghenghi et al. (2001) Endocrine 14:29; TH9507 (Tesamorelin, a growth hormone-releasing factor); POL7080 (a protegrin analog, an anti-microbial peptide); relaxin; a corticotropin releasing factor agonist such as urotensin, sauvagine, and the like; a heat shock protein derivative such as DiaPep277; a human immunodeficiency virus entry inhibitor; a heat shock protein-20 mimic such as AZX100; a thrombin receptor activating peptide such as TP508 (Chrysalin); a urocortin 2 mimic (e.g., a CRF2 agonist) such as urocortin-2; an immune activator such as Zadaxin (thymalfasin; thymosin-α1), see, e.g., Sjogren (2004) J. Gastroenterol. Hepatol. 19:S69; a hepatitis C virus (HCV) entry inhibitorE2 peptide such as HCV3; an atrial natriuretic peptide such as HANP (Sun 4936; carperitide); an annexin peptide; a defensin (anti-microbial peptide) such as hBD2-4; a defensin (anti-microbial peptide) such as hBD-3; a defensin (anti- microbial peptide) such as PMX-30063; a histatin (anti-microbial peptide) such as histatin-3, histatin-5, histatin-6, and histatin-9; a histatin (anti-microbial peptide) such as PAC-113; an indolicidin (anti-microbial peptide) such as MX-594AN (Omniganin; CLS001); an indolicidin (anti-microbial peptide) such as Omnigard (MBI-226; CPI-226); an anti-microbial peptide such as an insect cecropin; an anti-microbial peptide such as a lactoferrin (talactoferrin); an LL- 37/cathelicidin derivative (an anti-microbial peptide) such as P60.4 (OP-145); a magainin (an anti-microbial peptide) such as Pexiganan (MSI-78; Suponex); a protegrin (an anti-microbial peptide) such as IB-367 (Iseganan); an agan peptide; a beta-natriuretic peptide such as Natrecor, or Noratak (Nesiritide), or ularitide; bivalarudin (Angiomax), a thrombin inhibitor; a C peptide derivative; a calcitonin such as Miacalcin (Fortical); an enkephalin derivative; an erythropoiesis-stimulating peptide such as Hematide; a gap junction modulator such as Atty. Dkt: RDWD-048WO Danegaptide (ZP1609); a gastrin-releasing peptide; a ghrelin; a glucagon-like peptide; a glucagon-like peptide-2 analog such as ZP1846 or ZP1848; a glucosaminyl muramyl dipeptide such as GMDP; a glycopeptide antibiotic such as Oritavancin; a teicoplanin derivative such as Dalbavancin; a gonadotropin releasing hormone (GnRH) such as Zoladex (Lupon) or Triptorelin; a histone deacetylase (HDAC) inhibitor depsipeptide such as PM02734 (Irvalec); an integrin such as eptifibatide; an insulin analog such as Humulog; a kahalalide depsipeptide such as PM02734; a kallikrein inhibitor such as Kalbitor (ecallantide); an antibiotic such as Telavancin; a lipopeptide such as Cubicin or MX-2401; a lutenizing hormone releasing hormone (LHRH) such as goserelin; an LHRH synthetic decapeptide agonist analog such as Treistar (triptorelin pamoate); an LHRH such as Eligard; an M2 protein channel peptide inhibitor; metreleptin; a melanocortin receptor agonist peptide such as bremalanotide/PT-141; a melanocortin; a muramyl tripeptide such as Mepact (mifamurtide); a myelin basic protein peptide such as MBP 8298 (dirucotide); an N-type voltage-gated calcium channel blocker such as Ziconotide (Prialt); a parathyroid hormone peptide; a parathyroid analog such as 768974; a peptide hormone analog such as UGP281; a prostaglandin F2-α receptor inhibitor such as PDC31; a protease inhibitor such as PPL-100; surfaxin; a thromobspondin-1 (TSP-1) mimetic such as CVX-045 or ABT 510; a vasoactive intestinal peptide; vasopressin; a Y2R agonist peptide such as RG7089; obinepeptide; and TM30339. Drugs [00378] The payload conjugated to an antibody of the present disclosure may be any of a number of drugs. Exemplary drugs include small molecule drugs and peptide drugs. Thus, the present disclosure provides drug-antibody conjugates, where a drug is covalently linked to fGly of a converted tag of an Ig heavy chain of an antibody. [00379] “Small molecule drug” as used herein refers to a compound, e.g., an organic compound, which exhibits a pharmaceutical activity of interest and which is generally of a molecular weight of no greater than about 800 Da, or no greater than 2000 Da, but can encompass molecules of up to 5kDa and can be as large as about 10 kDa. A small inorganic molecule refers to a molecule containing no carbon atoms, while a small organic molecule refers to a compound containing at least one carbon atom. Atty. Dkt: RDWD-048WO [00380] “Peptide drug” as used herein refers to amino-acid containing polymeric compounds, and is meant to encompass naturally-occurring and non-naturally-occurring peptides, oligopeptides, cyclic peptides, polypeptides, and proteins, as well as peptide mimetics. The peptide drugs may be obtained by chemical synthesis or be produced from a genetically encoded source (e.g., recombinant source). Peptide drugs can range in molecular weight, and can be from 200 Da to 10 kDa or greater in molecular weight. [00381] In some cases, the drug is a cancer chemotherapeutic agent. For example, where an antibody has specificity for a tumor cell, the antibody can be modified as described herein to include an aldehyde tag, can be subsequently converted to an fGly-modified antibody, and can then be conjugated to a cancer chemotherapeutic agent. Cancer chemotherapeutic agents include non-peptidic (i.e., non-proteinaceous) compounds that reduce proliferation of cancer cells, and encompass cytotoxic agents and cytostatic agents. Non-limiting examples of chemotherapeutic agents include alkylating agents, nitrosoureas, antimetabolites, antitumor antibiotics, plant (vinca) alkaloids, and steroid hormones. Peptidic compounds can also be used. [00382] Suitable cancer chemotherapeutic agents include dolastatin and active analogs and derivatives thereof; and auristatin and active analogs and derivatives thereof. See, e.g., WO 96/33212, WO 96/14856, and USPN 6,323,315. For example, dolastatin 10 or auristatin PE can be included in an antibody-drug conjugate of the present disclosure. Suitable cancer chemotherapeutic agents also include maytansinoids and active analogs and derivatives thereof (see, e.g., EP 1391213; and Liu et al (1996) Proc. Natl. Acad. Sci. USA 93:8618-8623); and duocarmycins and active analogs and derivatives thereof (e.g., including the synthetic analogues, KW-2189 and CB 1-TM1). In some cases, the cancer chemotherapeutic agent includes a pyrrolobenzodiazepine compound. [00383] Agents that act to reduce cellular proliferation are known in the art and widely used. Such agents include alkylating agents, such as nitrogen mustards, nitrosoureas, ethylenimine derivatives, alkyl sulfonates, and triazenes, including, but not limited to, mechlorethamine, cyclophosphamide (Cytoxan™), melphalan (L-sarcolysin), carmustine (BCNU), lomustine (CCNU), semustine (methyl-CCNU), streptozocin, chlorozotocin, uracil Atty. Dkt: RDWD-048WO mustard, chlormethine, ifosfamide, chlorambucil, pipobroman, triethylenemelamine, triethylenethiophosphoramine, busulfan, dacarbazine, and temozolomide. [00384] Antimetabolite agents include folic acid analogs, pyrimidine analogs, purine analogs, and adenosine deaminase inhibitors, including, but not limited to, cytarabine (CYTOSAR-U), cytosine arabinoside, fluorouracil (5-FU), floxuridine (FudR), 6-thioguanine, 6- mercaptopurine (6-MP), pentostatin, 5-fluorouracil (5-FU), methotrexate, 10-propargyl-5,8- dideazafolate (PDDF, CB3717), 5,8-dideazatetrahydrofolic acid (DDATHF), leucovorin, fludarabine phosphate, pentostatine, and gemcitabine. [00385] Suitable natural products and their derivatives, (e.g., vinca alkaloids, antitumor antibiotics, enzymes, lymphokines, and epipodophyllotoxins), include, but are not limited to, Ara-C, paclitaxel (Taxol®), docetaxel (Taxotere®), deoxycoformycin, mitomycin-C, L- asparaginase, azathioprine; brequinar; alkaloids, e.g. vincristine, vinblastine, vinorelbine, vindesine, etc.; podophyllotoxins, e.g. etoposide, teniposide, etc.; antibiotics, e.g. anthracycline, daunorubicin hydrochloride (daunomycin, rubidomycin, cerubidine), idarubicin, doxorubicin, epirubicin and morpholino derivatives, etc.; phenoxizone biscyclopeptides, e.g. dactinomycin; basic glycopeptides, e.g. bleomycin; anthraquinone glycosides, e.g. plicamycin (mithramycin); anthracenediones, e.g. mitoxantrone; azirinopyrrolo indolediones, e.g. mitomycin; macrocyclic immunosuppressants, e.g. cyclosporine, FK-506 (tacrolimus, prograf), rapamycin, etc.; and the like. [00386] Other anti-proliferative cytotoxic agents are navelbene, CPT-11, anastrazole, letrazole, capecitabine, reloxafine, cyclophosphamide, ifosamide, and droloxafine. [00387] Microtubule affecting agents that have antiproliferative activity are also suitable for use and include, but are not limited to, auristatins (e.g., MMAE, MMAF), allocolchicine (NSC 406042), Halichondrin B (NSC 609395), colchicine (NSC 757), colchicine derivatives (e.g., NSC 33410), dolstatin 10 (NSC 376128), maytansine (NSC 153858), rhizoxin (NSC 332598), paclitaxel (Taxol®), Taxol® derivatives, docetaxel (Taxotere®), thiocolchicine (NSC 361792), trityl cysterin, vinblastine sulfate, vincristine sulfate, natural and synthetic epothilones including but not limited to, eopthilone A, epothilone B, discodermolide; estramustine, nocodazole, and the like. [00388] Hormone modulators and steroids (including synthetic analogs) that are suitable for use include, but are not limited to, adrenocorticosteroids, e.g. prednisone, dexamethasone, Atty. Dkt: RDWD-048WO etc.; estrogens and pregestins, e.g. hydroxyprogesterone caproate, medroxyprogesterone acetate, megestrol acetate, estradiol, clomiphene, tamoxifen; etc.; and adrenocortical suppressants, e.g. aminoglutethimide; 17α-ethinylestradiol; diethylstilbestrol, testosterone, fluoxymesterone, dromostanolone propionate, testolactone, methylprednisolone, methyl- testosterone, prednisolone, triamcinolone, chlorotrianisene, hydroxyprogesterone, aminoglutethimide, estramustine, medroxyprogesterone acetate, leuprolide, Flutamide (Drogenil), Toremifene (Fareston), and Zoladex®. Estrogens stimulate proliferation and differentiation; therefore compounds that bind to the estrogen receptor are used to block this activity. Corticosteroids may inhibit T cell proliferation. [00389] Other suitable chemotherapeutic agents include metal complexes, e.g. cisplatin (cis-DDP), carboplatin, etc.; ureas, e.g. hydroxyurea; and hydrazines, e.g. N-methylhydrazine; epidophyllotoxin; a topoisomerase inhibitor (e.g., SN-38, irinotecan, belotecan, exatecan, deruxtecan, or other camptothecins); procarbazine; mitoxantrone; leucovorin; tegafur; etc. Other anti-proliferative agents of interest include immunosuppressants, e.g. mycophenolic acid, thalidomide, desoxyspergualin, azasporine, leflunomide, mizoribine, azaspirane (SKF 105685); Iressa® (ZD 1839, 4-(3-chloro-4-fluorophenylamino)-7-methoxy-6-(3-(4- morpholinyl)propoxy)quinazoline); etc. [00390] Taxanes are suitable for use. “Taxanes” include paclitaxel, as well as any active taxane derivative or pro-drug. "Paclitaxel" (which should be understood herein to include analogues, formulations, and derivatives such as, for example, docetaxel, TAXOL^, TAXOTERE^ (a formulation of docetaxel), 10-desacetyl analogs of paclitaxel and 3'N-desbenzoyl-3'N-t- butoxycarbonyl analogs of paclitaxel) may be readily prepared utilizing techniques known to those skilled in the art (see also WO 94/07882, WO 94/07881, WO 94/07880, WO 94/07876, WO 93/23555, WO 93/10076; U.S. Pat. Nos.5,294,637; 5,283,253; 5,279,949; 5,274,137; 5,202,448; 5,200,534; 5,229,529; and EP 590,267), or obtained from a variety of commercial sources, including for example, Sigma Chemical Co., St. Louis, Mo. (T7402 from Taxus brevifolia; or T-1912 from Taxus yannanensis). [00391] Paclitaxel should be understood to refer to not only the common chemically available form of paclitaxel, but analogs and derivatives (e.g., Taxotere^ docetaxel, as noted above) and paclitaxel conjugates (e.g., paclitaxel-PEG, paclitaxel-dextran, or paclitaxel-xylose). Atty. Dkt: RDWD-048WO [00392] Also included within the term “taxane” are a variety of known derivatives, including both hydrophilic derivatives, and hydrophobic derivatives. Taxane derivatives include, but not limited to, galactose and mannose derivatives described in International Patent Application No. WO 99/18113; piperazino and other derivatives described in WO 99/14209; taxane derivatives described in WO 99/09021, WO 98/22451, and U.S. Patent No. 5,869,680; 6-thio derivatives described in WO 98/28288; sulfenamide derivatives described in U.S. Patent No.5,821,263; and taxol derivative described in U.S. Patent No.5,415,869. It further includes prodrugs of paclitaxel including, but not limited to, those described in WO 98/58927; WO 98/13059; and U.S. Patent No.5,824,701. [00393] Biological response modifiers suitable for use include, but are not limited to, (1) inhibitors of tyrosine kinase (RTK) activity; (2) inhibitors of serine/threonine kinase activity; (3) tumor-associated antigen antagonists, such as antibodies that bind specifically to a tumor antigen; (4) apoptosis receptor agonists; (5) interleukin-2; (6) IFN-α; (7) IFN-γ; (8) colony- stimulating factors; and (9) inhibitors of angiogenesis. FC RECEPTOR BINDING [00394] An antibody conjugate, and/or an fGly-modified but unconjugated antibody, of the present disclosure may show increased or reduced binding to one or more Fcγ receptors (e.g., CD16a, CD64, FcRn, etc.) compared to its parent antibody that does not include a tag sequence. In some embodiments, the antibody conjugate, and/or the fGly-modified but unconjugated antibody, binds less effectively to one or more Fcγ receptors (e.g., CD16a and/or CD64) than its parent antibody that does not include a tag sequence in its Ig heavy chain constant region. Certain such antibodies are described in U.S. Patent Nos.11,466,096 and 11,208,632, which are herein incorporated by reference in their entireties. F^ORMULATIONS [00395] The antibody conjugates of the present disclosure can be formulated in a variety of different ways. In general, where the antibody conjugate is an antibody-drug conjugate, the antibody conjugate is formulated in a manner compatible with the drug conjugated to the Ig Atty. Dkt: RDWD-048WO heavy and/or light chains, the condition to be treated, and the route of administration to be used. [00396] The antibody conjugate (e.g., antibody-drug conjugate) can be provided in any suitable form, e.g., in the form of a pharmaceutically acceptable salt, and can be formulated for any suitable route of administration, e.g., oral, topical or parenteral administration. Where the antibody conjugate is provided as a liquid injectable (such as in those embodiments where they are administered intravenously or directly into a tissue), the antibody conjugate can be provided as a ready-to-use dosage form, or as a reconstitutable storage-stable powder or liquid composed of pharmaceutically acceptable carriers and excipients. [00397] Methods for formulating antibody conjugates can be adapted from those available in the art. For example, antibody conjugates can be provided in a pharmaceutical composition comprising an effective amount of an antibody conjugate and a pharmaceutically acceptable carrier (e.g., saline). The pharmaceutical composition may optionally include other additives (e.g., buffers, stabilizers, preservatives, and the like). Of particular interest in some embodiments are formulations that are suitable for administration to a mammal, particularly those that are suitable for administration to a human. N^UCLEIC A^CIDS, E^XPRESSION V^{ECTORS AND} H^OST C^ELLS [00398] The present disclosure provides a nucleic acid encoding Ig heavy chain and/or Ig light chain containing one or more tags, as well as constructs and host cells containing the nucleic acid. Such nucleic acids comprise a sequence of DNA having an open reading frame that encodes a tagged Ig heavy chain and/or Ig light chain and, in most embodiments, is capable, under appropriate conditions, of being expressed. “Nucleic acid” encompasses DNA, cDNA, mRNA, and vectors comprising such nucleic acids. [00399] In some cases, a nucleic acid comprises a first open reading frame, which encodes for an Ig heavy chain, which contains one or more tags and a second open reading frame, which encodes for an Ig light chain, which may or may not contain a tag. When such nucleic acid is expressed, it encodes for both chains of the resulting antibodies having two or more tags in the Ig heavy chain and/or Ig light chain. Atty. Dkt: RDWD-048WO [00400] The present disclosure provides a recombinant nucleic acid comprising a nucleotide sequence encoding a tagged antibodies, as described above. The recombinant nucleic acid can include: [00401] 1) a nucleotide sequence encoding a tagged Ig heavy chain constant region (and not an Ig heavy chain variable region, i.e., where the recombinant nucleic acid lacks a nucleotide sequence encoding an Ig V_H domain); [00402] 2) a nucleotide sequence encoding a tagged Ig, where the Ig comprises an Ig V_H domain and a tagged Ig heavy chain constant region; [00403] 3) a nucleotide sequence encoding a tagged or untagged Ig light chain constant region (and not an Ig light chain variable region, i.e., where the recombinant nucleic acid lacks a nucleotide sequence encoding an Ig VL domain); and a nucleotide sequence encoding a tagged Ig heavy chain constant region (and not an Ig heavy chain variable region, i.e., where the recombinant nucleic acid lacks a nucleotide sequence encoding an Ig VH domain); [00404] 4) a nucleotide sequence encoding a tagged Ig heavy chain constant region, as described above, (and not an Ig heavy chain variable region, i.e., where the recombinant nucleic acid lacks a nucleotide sequence encoding an Ig VH domain); and a nucleotide sequence encoding a tagged or untagged Ig light chain constant region (and not an Ig light chain variable region, i.e., where the recombinant nucleic acid lacks a nucleotide sequence encoding an Ig VL domain); [00405] 5) a nucleotide sequence encoding a first tagged Ig, where the first aldehyde- tagged Ig comprises an Ig VH domain and a tagged Ig heavy chain constant region; and a nucleotide sequence encoding a second tagged Ig, where the second tagged Ig comprises an Ig VL domain and a tagged or untagged Ig light chain constant region; [00406] 6) a nucleotide sequence encoding a first Ig, where the first Ig comprises an Ig VH domain and a tagged Ig heavy chain constant region; and a nucleotide sequence encoding a second Ig, where the second Ig comprises an Ig VL domain and a tagged or untagged Ig light chain constant region. [00407] The present disclosure also provides a recombinant expression vector comprising a nucleic acid as described above, where the nucleotide sequence encoding the Ig(s) is operably linked to a promoter. In some embodiments, where a subject recombinant Atty. Dkt: RDWD-048WO expression vector encodes both Ig heavy and light chains (with or without Ig variable regions), the heavy and light chain-encoding sequences can be operably linked to the same promoter, or to separate promoters. [00408] Where a recombinant expression vector includes a nucleotide sequence encoding a heavy chain variable (V_H) region and/or a light chain variable (V_L) region, it will be appreciated that a large number of V_H and V_L amino acid sequences, and nucleotide sequences encoding same, are known in the art, and can be used. See, e.g., Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md. (1991). [00409] In those instances in which a recombinant expression vector comprises a nucleotide sequence encoding an Ig heavy or Ig light chain without variable region sequences, the vector can include an insertion site for an Ig variable region 5’ of the Ig-encoding nucleotide sequence. For example, a recombinant expression vector can comprise, in order from 5’ to 3’: [00410] 1) an insertion site for a nucleotide sequence encoding a VL domain; and a nucleotide sequence encoding an Ig light chain constant region, which may or may not include tag; or [00411] 2) an insertion site for a nucleotide sequence encoding a VH domain; and a nucleotide sequence encoding a tagged Ig heavy chain constant region. [00412] Nucleic acids contemplated herein can be provided as part of a vector (also referred to as a construct), a wide variety of which are known in the art. Exemplary vectors include, but are not limited to, plasmids; cosmids; viral vectors (e.g., retroviral vectors); non- viral vectors; artificial chromosomes (yeast artificial chromosomes (YAC’s), BAC’s, etc.); mini- chromosomes; and the like. The choice of vector will depend upon a variety of factors such as the type of cell in which propagation is desired and the purpose of propagation. [00413] Vectors can provide extrachromosomal maintenance in a host cell or can provide integration into the host cell genome. Vectors are amply described in numerous publications well known to those in the art, including, e.g., Short Protocols in Molecular Biology, (1999) F. Ausubel, et al., eds., Wiley & Sons. Vectors may provide for expression of the Atty. Dkt: RDWD-048WO nucleic acids encoding a polypeptide of interest (e.g., a tagged polypeptide, an FGE, etc.), may provide for propagating the subject nucleic acids, or both. [00414] Exemplary vectors that may be used include but are not limited to those derived from recombinant bacteriophage DNA, plasmid DNA or cosmid DNA. For example, plasmid vectors such as pBR322, pUC 19/18, pUC 118, 119 and the M13 mp series of vectors may be used. Bacteriophage vectors may include λgt10, λgt11, λgt18-23, λZAP/R and the EMBL series of bacteriophage vectors. Cosmid vectors that may be utilized include, but are not limited to, pJB8, pCV 103, pCV 107, pCV 108, pTM, pMCS, pNNL, pHSG274, COS202, COS203, pWE15, pWE16 and the charomid 9 series of vectors. Alternatively, recombinant virus vectors may be engineered, including but not limited to those derived from viruses such as herpes virus, retroviruses, vaccinia virus, poxviruses, adenoviruses, adeno-associated viruses, or bovine papilloma virus. [00415] For expression of a protein of interest (e.g., a tagged Ig or an FGE), an expression cassette may be employed. Thus, the present invention provides a recombinant expression vector comprising a subject nucleic acid. The expression vector provides a transcriptional and translational regulatory sequence, and may provide for inducible or constitutive expression, where the coding region is operably linked under the transcriptional control of the transcriptional initiation region, and a transcriptional and translational termination region. These control regions may be native to the gene encoding the polypeptide (e.g., the Ig or the FGE), or may be derived from exogenous sources. In general, the transcriptional and translational regulatory sequences may include, but are not limited to, promoter sequences, ribosomal binding sites, transcriptional start and stop sequences, translational start and stop sequences, and enhancer or activator sequences. In addition to constitutive and inducible promoters, strong promoters (e.g., T7, CMV, and the like) find use in the constructs described herein, particularly where high expression levels are desired in an in vivo (cell-based) or in an in vitro expression system. Further exemplary promoters include mouse mammary tumor virus (MMTV) promoters, Rous sarcoma virus (RSV) promoters, adenovirus promoters, the promoter from the immediate early gene of human CMV (Boshart et al., Cell 41:521-530, 1985), and the promoter from the long terminal repeat (LTR) of RSV Atty. Dkt: RDWD-048WO (Gorman et al., Proc. Natl. Acad. Sci. USA 79:6777-6781, 1982). The promoter can also be provided by, for example, a 5’UTR of a retrovirus. [00416] Expression vectors generally have convenient restriction sites located near the promoter sequence to provide for the insertion of nucleic acid sequences encoding proteins of interest. A selectable marker operative in the expression host may be present to facilitate selection of cells containing the vector. In addition, the expression construct may include additional elements. For example, the expression vector may have one or two replication systems, thus allowing it to be maintained in organisms, for example in mammalian or insect cells for expression and in a prokaryotic host for cloning and amplification. In addition the expression construct may contain a selectable marker gene to allow the selection of transformed host cells. Selection genes are well known in the art and will vary with the host cell used. [00417] Expression constructs encoding tagged Ig can also be generated using amplification methods (e.g., a polymerase chain reaction (PCR)), where at least one amplification primer (i.e., at least one of a forward or reverse primer) includes a nucleic acid sequence encoding an aldehyde tag. For example, an amplification primer having a tag amino acid sequence-encoding nucleotide sequence is designed to provide for amplification of a nucleic acid encoding an Ig. The extension product that results from polymerase-mediated synthesis from the tagged forward primer produces a nucleic acid amplification product encoding a fusion protein composed of a tagged Ig. The amplification product is then inserted into an expression construct of choice to provide a tagged polypeptide expression construct. Host cells [00418] The present disclosure provides genetically modified host cells comprising a subject nucleic acid, including a genetically modified host cell comprising a recombinant expression vector as described above. Any of a number of suitable host cells can be used in the production of an antibody containing the present tagged Ig heavy chain. The host cell used for production of an antibody containing the tagged Ig can optionally provide for FGE-mediated conversion, so that the antibody produced contains an fGly-modified Ig, where the tag is converted to contain fGly, following expression and modification by FGE. Alternatively the host Atty. Dkt: RDWD-048WO cell can provide for production of an antibody containing a tagged and unconverted Ig heavy chain (e.g., due to lack of expression of an FGE that facilitates conversion of the tag). [00419] The aldehyde moiety of a converted tag can be used for a variety of applications including, but not limited to, visualization using fluorescence or epitope labeling (e.g., electron microscopy using gold particles equipped with aldehyde reactive groups); protein immobilization (e.g., protein microarray production); protein dynamics and localization studies and applications; and conjugation of proteins with a payload (e.g., moieties that improve a parent protein's half-life (e.g., poly(ethylene glycol)), targeting moieties (e.g., to enhance delivery to a site of action), and biologically active moieties (e.g., a therapeutic moiety). [00420] In general, the polypeptides described herein may be expressed in prokaryotes or eukaryotes in accordance with conventional ways, depending upon the purpose for expression. Thus, the present invention further provides a host cell, e.g., a genetically modified host cell that comprises a nucleic acid encoding a tagged polypeptide. The host cell can further optionally comprise a recombinant FGE, which may be endogenous or heterologous to the host cell. Thus, in some cases, the host cell is genetically modified to express an FGE. [00421] Host cells for production (including large scale production) of a tagged and unconverted, or (where the host cell expresses a suitable FGE) tagged and converted Ig, or for production of an FGE (e.g., for use in a cell-free method) can be selected from any of a variety of available host cells. Exemplary host cells include those of a prokaryotic or eukaryotic unicellular organism, such as bacteria (e.g., Escherichia coli strains, Bacillus spp. (e.g., B. subtilis), and the like) yeast or fungi (e.g., S. cerevisiae, Pichia spp., and the like), and other such host cells can be used. Exemplary host cells originally derived from a higher organism such as insects, vertebrates, particularly mammals, (e.g. CHO, HEK, and the like), may be used as the expression host cells. [00422] Suitable mammalian cell lines include, but are not limited to, HeLa cells (e.g., American Type Culture Collection (ATCC) No. CCL-2), CHO cells (e.g., ATCC Nos. CRL9618 and CRL9096), CHO DG44 cells (Urlaub (1983) Cell 33:405), CHO-K1 cells (ATCC CCL-61), 293 cells (e.g., ATCC No. CRL-1573), Vero cells, NIH 3T3 cells (e.g., ATCC No. CRL-1658), Huh-7 cells, BHK cells (e.g., ATCC No. CCL10), PC12 cells (ATCC No. CRL1721), COS cells, COS-7 cells (ATCC No. Atty. Dkt: RDWD-048WO CRL1651), RAT1 cells, mouse L cells (ATCC No. CCLI.3), human embryonic kidney (HEK) cells (ATCC No. CRL1573), HLHepG2 cells, and the like. [00423] Specific expression systems of interest include bacterial, yeast, insect cell and mammalian cell derived expression systems. Representative systems from each of these categories are provided below. [00424] The product can be recovered by any appropriate means known in the art. Further, any convenient protein purification procedures may be employed, where suitable protein purification methodologies are described in Guide to Protein Purification, (Deuthser ed.) (Academic Press, 1990). For example, a lysate may be prepared from a cell comprising the expression vector expressing the tagged Ig, and purified using high performance liquid chromatography (HPLC), exclusion chromatography, gel electrophoresis, affinity chromatography, and the like. M^ETHODS Methods for Conversion and Modification of a Tag [00425] Conversion of a tag, e.g., a sulfatase motif in a tag, present in a tagged Ig of an antibody can be accomplished by cell-based (in vivo) or cell-free methods (in vitro). Similarly, modification of a converted tag of a tagged polypeptide can be accomplished by cell-based (in vivo) or cell-free methods (in vitro). These are described in more detail below. “In vivo” Host Cells Conversion and Modification [00426] Conversion of a tag, e.g., a sulfatase motif in a tag, of an aldehyde tagged polypeptide of an antibody can be accomplished by expression of the tagged polypeptide in a cell that contains a suitable FGE. In this embodiment, conversion of the cysteine or serine of the tag occurs during or following translation in the host cell. The FGE of the host cell can be endogenous to the host cell, or the host cell can be recombinant for a suitable FGE that is heterologous to the host cell. FGE expression can be provided by an expression system endogenous to the FGE gene (e.g., expression is provided by a promoter and other control elements present in the native FGE gene of the host cell), or can be provided by from a Atty. Dkt: RDWD-048WO recombinant expression system in which the FGE coding sequence is operably linked to a heterologous promoter to provide for constitutive or inducible expression. [00427] In some instances, where the present method is carried out in a cell, the cell is in vitro, e.g., in in vitro cell culture, e.g., where the cell is cultured in vitro in a single-cell suspension or as an adherent cell. In some embodiments, the cell is cultured in the presence of an oxidation reagent that can activate FGE. In some embodiments, a cell expressing an FGE is cultured in the presence of a suitable amount of Cu²⁺ in the culture medium. In certain aspects, the Cu²⁺ is present in the cell culture medium at a concentration of from 1 nM to 100 mM, such as from 0.1 μM to 10 mM, from 1 μM to 1 mM, from 2 μM to 500 μM, from 4 μM to 300 μM, or from 5 μM to 200 μM (e.g., from 10 μM to 150 μM). The culture medium may be supplemented with any suitable copper salt to provide for the Cu²⁺. Suitable copper salts include, but are not limited to, copper sulfate (i.e., copper(II) sulfate, CuSO4), copper citrate, copper tartrate, copper nitrate, and any combination thereof. “In vitro” (Cell-Free) Conversion and Modification [00428] In vitro (cell-free) conversion of a tag, e.g., a sulfatase motif in a tag, of a tagged Ig of an antibody can be accomplished by contacting a tagged polypeptide with an FGE under conditions suitable for conversion of a cysteine or serine of a sulfatase motif of the tag to an fGly. For example, nucleic acid encoding a tagged Ig can be expressed in an in vitro transcription/translation system in the presence of a suitable FGE to provide for production of tagged and converted Ig. [00429] Alternatively, isolated, unconverted, tagged Ig can be isolated following recombinant production in a host cell lacking a suitable FGE or by synthetic production. The isolated tagged Ig is then contacted with a suitable FGE under conditions to provide for tag conversion. The tagged Ig can be unfolded by methods known in the art (e.g., using heat, adjustment of pH, chaotropic agents, (e.g., urea, and the like), organic solvents (e.g., hydrocarbons: octane, benzene, chloroform), etc.) and the denatured protein contacted with a suitable FGE. The tagged Ig can then be refolded under suitable conditions. [00430] With respect to modification of tagged and converted Ig of an antibody, e.g., to covalently and site-specifically attach a payload (e.g., drug) thereto, modification is normally Atty. Dkt: RDWD-048WO carried out in vitro. An antibody containing a converted aldehyde tagged Ig is isolated from a production source (e.g., recombinant host cell production, synthetic production), and contacted with a reactive partner-containing drug or other moiety under conditions suitable to provide for conjugation of the drug or other moiety to the fGly of the tag in the Ig, e.g., Ig heavy chain, of the antibody. [00431] In some instances, a combination of cell-based conversion and cell-free conversion is carried out, to generate a converted tag; followed by cell-free modification of the converted tag. In some embodiments, a combination of cell-free conversion and cell-based conversion is carried out. Method of Producing an Antibody Conjugate [00432] Aspects of the present disclosure include a method of producing an antibody conjugate, as described herein. In general terms, the method may include combining, in a reaction mixture, an fGly-modified antibody having a converted tag in its Ig heavy chain, as described above, and a reactive partner, e.g., an aldehyde-reactive reactive partner, that includes the payload (e.g., drug) and an aldehyde-reactive group. In some cases, the reactive partner may be represented by the formula: P-(L)-R, where P is the payload covalently linked to R, an aldehyde-reactive group, through an optional linking group L. Under suitable conditions, the aldehyde-reactive group may react with the aldehyde group of the fGly in the converted tag of the fGly-modified antibody (“A”) in the reaction mixture, to form a covalent linkage between the payload (e.g., drug) and the fGly-modified antibody at the fGly residue of the converted tag (which may be represented by the formula: P-(L)-A, or P-(L)-A-(L)-P, etc., depending on the number of tags present in each of the Ig of the antibody). The reaction may be carried out in any suitable condition, such as those described in, e.g., US20120183566, US20140141025 and WO2014074218, each of which is incorporated herein by reference. [00433] The payload (P) may be any suitable moiety (e.g., drug, water-soluble polymer, detectable label, synthetic peptide, etc.) as described above, and may be a compound that can be functionalized with an aldehyde-reactive group. The aldehyde-reactive group (R) may be any suitable functional group suitable for carrying out a conjugation reaction between the present fGly-modified antibody and the reactive partner. In some cases, the aldehyde-reactive Atty. Dkt: RDWD-048WO group is an α-nucleophile, such as an aminooxy or hydrazide group. Suitable aldehyde-reactive groups include, without limitation, a hydrazine compound, hydrazide compound, aminooxy compound, semicarbazide (e.g., thiosemicarbazide) compound, hydrazinyl-indole compound, hydrazinyl-imidazole compound, hydrazinyl-pyrrole compound, hydrazinyl-furan compound, and a pyrazalinone compound. [00434] In some embodiments, the reactive partner includes a payload (P) (e.g., drug ) attached to an aldehyde-reactive group (R) that is based on a hydrazinyl-indole group, and can be produced using any suitable method, e.g., as described in US20140141025, which is incorporated herein by reference. A hydrazinyl-indole-containing reactive partner may react with an aldehyde of fGly in a converted tag in an fGly-modified antibody, as described herein, where the hydrazine of the hydrazinyl-indole coupling moiety undergoes an intramolecular cyclization to form a partially unsaturated pyrazole or pyridazine ring, to covalently attach the payload (e.g., drug) to the antibody Ig heavy chain. Alternatively, the hydrazine of the hydrazinyl-indole coupling moiety may undergo an intramolecular cyclization to form a partially unsaturated pyridazine or 1,2-diazepine ring, to covalently attach the payload (e.g., drug) to the antibody Ig heavy chain. [00435] In some cases, the reactive partner includes a payload (P) (e.g., drug) attached to an aldehyde-reactive group (R) based on a pyrazalinone group, and can be produced using any suitable method, e.g., as described in WO2014074218, which is incorporated herein by reference. A pyrazalinone-containing reactive partner may react with an aldehyde of fGly in a converted tag in an fGly-modified antibody, as described herein, to covalently attach the payload (e.g., drug) of the reactive partner to the antibody Ig heavy chain through a cyclic linkage. [00436] In some cases, the reactive partner includes a payload (P) (e.g., drug ) attached to an aldehyde-reactive group (R) based on a hydrazinyl-substituted heteroaryl ring compound, such as a hydrazinyl-substituted 5-membered heteroaryl ring compound, where one or more atoms in the ring is a heteroatom (e.g., N, O or S). The hydrazinyl-substituted heteroaryl ring compound may include a hydrazinyl-imidazole compound, hydrazinyl-pyrrole compound, or a hydrazinyl-furan compound. Thus, a hydrazinyl-substituted heteroaryl ring compound (e.g., a hydrazinyl-imidazole compound, hydrazinyl-pyrrole compound, a hydrazinyl-furan compound) Atty. Dkt: RDWD-048WO may react with an aldehyde of fGly in a converted tag in an fGly-modified antibody, as described herein, to covalently attach the payload (e.g., drug) to the antibody Ig heavy chain through a cyclic linkage. [00437] The reactive partner may further include a linking group (L) bridging the payload (P) (e.g., drug ) and the aldehyde-reactive group (R) through covalent bonds. The linking group may be any suitable linking group. In some cases, the linking group includes polyethylene glycol (PEG); amino acids; alkyl groups, including substituted alkyl groups; a protease cleavable group; esters; acyloxy groups, including substituted acyloxy groups, etc. Suitable linking groups and methods of using the same to bridge a payload (e.g., drug) and an aldehyde-reactive group are described in, e.g., US20150157736, which is incorporated by reference herein. In some embodiments, the linking group includes a 4-aminopiperidine (4AP) derivative. [00438] In some cases, the payload is a drug, e.g., a peptide drug. In some cases, peptide drugs to be conjugated to a tagged and converted Ig of an fGly-modified antibody can be modified to incorporate an aldehyde-reactive group for reaction with an aldehyde of the fGly residue of the tagged and converted Ig. Since the methods of tagged and converted polypeptide modification are compatible with conventional chemical processes, any of a wide variety of commercially available reagents can be used to accomplish conjugation. For example, aminooxy, hydrazide, hydrazine, thiosemicarbazide, hydrazinyl-indole, hydrazinyl- imidazole, hydrazinyl-pyrrole, hydrazinyl-furan or pyrazalinone derivatives of a number of moieties of interest are suitable reactive partners, and are readily available or can be generated using standard chemical methods. [00439] Where the drug is a peptide drug, the reactive moiety (e.g., aminooxy or hydrazide can be positioned at an N-terminal region, the N-terminus, a C-terminal region, the C-terminus, or at a position internal to the peptide. For example, one method involves synthesizing a peptide drug having an aminooxy group. In this example, the peptide is synthesized from a Boc-protected precursor. An amino group of a peptide can react with a compound comprising a carboxylic acid group and oxy-N-Boc group. As an example, the amino group of the peptide reacts with 3-(2,5-dioxopyrrolidin-1-yloxy)propanoic acid. Other variations on the compound comprising a carboxylic acid group and oxy-N-protecting group can include different number of carbons in the alkylene linker and substituents on the alkylene Atty. Dkt: RDWD-048WO linker. The reaction between the amino group of the peptide and the compound comprising a carboxylic acid group and oxy-N-protecting group occurs through standard peptide coupling chemistry. Examples of peptide coupling reagents that can be used include, but not limited to, DCC (dicyclohexylcarbodiimide), DIC (diisopropylcarbodiimide), di-p-toluoylcarbodiimide, BDP (1-benzotriazole diethylphosphate-1-cyclohexyl-3-(2-morpholinylethyl)carbodiimide), EDC (1- (3-dimethylaminopropyl-3-ethyl-carbodiimide hydrochloride), cyanuric fluoride, cyanuric chloride, TFFH (tetramethyl fluoroformamidinium hexafluorophosphosphate), DPPA (diphenylphosphorazidate), BOP (benzotriazol-1-yloxytris(dimethylamino)phosphonium hexafluorophosphate), HBTU (O-benzotriazol-1-yl-N,N,N',N'-tetramethyluronium hexafluorophosphate), TBTU (O-benzotriazol-1-yl-N,N,N',N'-tetramethyluronium tetrafluoroborate), TSTU (O-(N-succinimidyl)-N,N,N',N'-tetramethyluronium tetrafluoroborate), HATU (N-[(dimethylamino)-1-H-1,2,3-triazolo[4,5,6]-pyridin-1- ylmethylene]- -N-methylmethanaminium hexafluorophosphate N-oxide), BOP-Cl (bis(2-oxo-3- oxazolidinyl)phosphinic chloride), PyBOP ((1-H-1,2,3-benzotriazol-1-yloxy)- tris(pyrrolidino)phosphonium tetrafluorophopsphate), BrOP (bromotris(dimethylamino)phosphonium hexafluorophosphate), DEPBT (3- (diethoxyphosphoryloxy)-1,2,3-benzotriazin-4(3H)-one) PyBrOP (bromotris(pyrrolidino)phosphonium hexafluorophosphate). As a non-limiting example, HOBt and DIC can be used as peptide coupling reagents. [00440] Deprotection to expose the amino-oxy functionality is performed on the peptide comprising an N-protecting group. Deprotection of the N-oxysuccinimide group, for example, occurs according to standard deprotection conditions for a cyclic amide group. Deprotecting conditions can be found in Greene and Wuts, Protective Groups in Organic Chemistry, 3rd Ed., 1999, John Wiley & Sons, NY and Harrison et al. Certain deprotection conditions include a hydrazine reagent, amino reagent, or sodium borohydride. Deprotection of a Boc protecting group can occur with TFA. Other reagents for deprotection include, but are not limited to, hydrazine, methylhydrazine, phenylhydrazine, sodium borohydride, and methylamine. The product and intermediates can be purified by conventional means, such as HPLC purification. [00441] The ordinarily skilled artisan will appreciate that factors such as pH and steric hindrance (i.e., the accessibility of the aldehyde tag to reaction with a reactive partner of Atty. Dkt: RDWD-048WO interest) are of importance. Modifying reaction conditions to provide for optimal conjugation conditions is well within the skill of the ordinary artisan, and is routine in the art. In general, it is normally desirable to conduct conjugation reactions at a pH below 7, with a pH of about 5.5, about 6, about 6.5, usually about 5.5 being optimal. Where conjugation is conducted with a tagged and converted polypeptide present in or on a living cell, the conditions are selected so as to be physiologically compatible. For example, the pH can be dropped temporarily for a time sufficient to allow for the reaction to occur but within a period tolerated by the cell having an aldehyde tag (e.g., from about 30 min to 1 hour). Physiological conditions for conducting modification of tagged and converted polypeptides on a cell surface can be similar to those used in a ketone-azide reaction in modification of cells bearing cell-surface azides (see, e.g., US 6,570,040). [00442] Small molecule compounds containing, or modified to contain, an α- nucleophilic group that serves as a reactive partner with an aldehyde of an fGly of a converted tag are also contemplated for use as drugs in the Ig-drug conjugates of the present disclosure. General methods are known in the art for chemical synthetic schemes and conditions useful for synthesizing a compound of interest (see, e.g., Smith and March, March's Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, Fifth Edition, Wiley-Interscience, 2001; or Vogel, A Textbook of Practical Organic Chemistry, Including Qualitative Organic Analysis, Fourth Edition, New York: Longman, 1978). [00443] Thus small molecules having an aminooxy or hydrazone group for reaction with an aldehyde of an fGly of a tagged and converted Ig are available or can be readily synthesized. An aminooxy or hydrazone group can be installed onto a small molecule using standard synthetic chemistry techniques. Methods of Treating [00444] The antibody-drug conjugates of the present disclosure find use in treatment of a condition or disease in a subject that is amenable to treatment by administration of the parent drug (i.e., the drug prior to conjugation to the antibody). By “treatment” is meant that at least an amelioration of the symptoms associated with the condition afflicting the host is achieved, where amelioration is used in a broad sense to refer to at least a reduction in the Atty. Dkt: RDWD-048WO magnitude of a parameter, e.g. symptom, associated with the condition being treated. As such, treatment also includes situations where the pathological condition, or at least symptoms associated therewith, are completely inhibited, e.g., prevented from happening, or stopped, e.g. terminated, such that the host no longer suffers from the condition, or at least the symptoms that characterize the condition. Thus treatment includes: (i) prevention, that is, reducing the risk of development of clinical symptoms, including causing the clinical symptoms not to develop, e.g., preventing disease progression to a harmful state; (ii) inhibition, that is, arresting the development or further development of clinical symptoms, e.g., mitigating or completely inhibiting an active disease; and/or (iii) relief, that is, causing the regression of clinical symptoms. [00445] In the context of cancer, the term “treating” includes any or all of: reducing growth of a solid tumor, inhibiting replication of cancer cells, reducing overall tumor burden, and ameliorating one or more symptoms associated with a cancer. Thus, the present disclosure provides methods for delivering a cancer chemotherapeutic agent to an individual having a cancer. The methods are useful for treating a wide variety of cancers, including carcinomas, sarcomas, leukemias, and lymphomas. The cancer treated by the present method may be a cancer of a variety of tissues organs, such as, without limitation, cancer of the lungs, liver, breast, prostate, ovary, kidney, brain, colon, intestine, spleen, stomach, mouth, throat, skin, blood cells, etc. [00446] The antibody to which the payload, e.g., drug, such as a cancer chemotherapeutic agent, is bound may specifically bind to an antigen associated with cell(s) or tissue(s) that are to be targeted and acted upon by the payload. [00447] The present method may include administering to an individual a therapeutically effective amount of an antibody conjugate, e.g., an antibody-drug conjugate, as described herein. The antibody conjugate may be in any suitable formulation, e.g., formulated with a pharmaceutically acceptable excipient, as described herein. [00448] The subject to be treated can be one that needs a therapy, where the host to be treated is one amenable to treatment using the parent drug. Accordingly, a variety of subjects may be amenable to treatment using an antibody-drug conjugates disclosed herein. Generally such subjects are “mammals,” with humans being of particular interest. Other subjects can Atty. Dkt: RDWD-048WO include domestic pets (e.g., dogs and cats), livestock (e.g., cows, pigs, goats, horses, and the like), rodents (e.g., mice, guinea pigs, and rats, e.g., as in animal models of disease), as well as non-human primates (e.g., chimpanzees, and monkeys. [00449] The amount of antibody-drug conjugate administered can be initially determined based on guidance of a dose and/or dosage regimen of the parent drug. In general, the antibody-drug conjugates can provide for targeted delivery and/or enhanced serum half-life of the bound drug, thus providing for at least one of reduced dose or reduced administrations in a dosage regimen. Thus the antibody-drug conjugates can provide for reduced dose and/or reduced administration in a dosage regimen relative to the parent drug prior to being conjugated in an Ig-drug conjugate of the present disclosure. [00450] Furthermore, as noted above, because the antibody-drug conjugates can provide for controlled stoichiometry of drug delivery, dosages of antibody-drug conjugates can be calculated based on the number of drug molecules provided on a per antibody-drug conjugate basis. [00451] In some embodiments, multiple doses of an antibody-drug conjugate are administered. The frequency of administration of an antibody-drug conjugate can vary depending on any of a variety of factors, e.g., severity of the symptoms, etc. For example, in some embodiments, an Ig-drug conjugate is administered once per month, twice per month, three times per month, every other week (qow), once per week (qw), twice per week (biw), three times per week (tiw), four times per week, five times per week, six times per week, every other day (qod), daily (qd), twice a day (qid), or three times a day (tid). E^XAMPLES [00452] The following examples are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how to make and use the disclosed subject matter, and are not intended to limit the scope of what the inventors regard as their invention nor are they intended to represent that the experiments below are all or the only experiments performed. Efforts have been made to ensure accuracy with respect to numbers used (e.g. amounts, temperature, etc.) but some experimental errors and deviations should be accounted for. Unless indicated otherwise, parts are parts by weight, molecular weight is Atty. Dkt: RDWD-048WO weight average molecular weight, temperature is in degrees Celsius, and pressure is at or near atmospheric. Standard abbreviations may be used, e.g., bp, base pair(s); kb, kilobase(s); pl, picoliter(s); s or sec, second(s); min, minute(s); h or hr, hour(s); aa, amino acid(s); kb, kilobase(s); bp, base pair(s); nt, nucleotide(s); i.m., intramuscular(ly); i.p., intraperitoneal(ly); s.c., subcutaneous(ly); and the like. Example 1: Chemical Synthesis of Payload Linkers Material and Methods [00453] Synthetic reagents were purchased from Sigma-Aldrich, Acros, AK Scientific, or other commercial sources and were used without purification. Anhydrous solvents were obtained from commercial sources in sealed bottles. Compounds 1, 6, 16, 20, 33, and 37 were obtained commercially from Shanghai Medicilon and used without purification. Cytotoxic payloads 2 and 7 were purchased from commercial sources and used as received. Peptide 38 was obtained commercially from AnaSpec Inc. and used as received. In all cases, solvent was removed under reduced pressure with a Buchi Rotovapor R-114 equipped with a Buchi V-700 vacuum pump. Column chromatography was performed using a Biotage chromatography system. Preparative HPLC purifications were performed using Waters preparative HPLC unit equipped with Phenomenex Kinetex 5 µm EVO C18150 x 21.2 mm column. HPLC analyses were conducted on an Agilent 1100 Series Analytical HPLC equipped with a Model G1322A Degasser, Model G1311A Quarternary Pump, Model G1329A Autosampler, Model G1314 Variable Wavelength Detector, Agilent Poroshell 120 SB C18, 4.6 mm x 50 mm column at room temperature using a 10-100% gradient of water and acetonitrile containing 0.05% trifluoroacetic acid. HPLCs were monitored at 254 or 205 nm. Low-resolution mass spectra (LRMS) were acquired on Agilent Technology 6120 Quadrupole LC/MS, equipped with Agilent 1260 Infinity HPLC system, G1314 variable wavelength detector, and Agilent Poroshell 120 SB C18, 4.6 mm x 50 mm column at room temperature using 10-100% gradient of water and acetonitrile containing 0.1% formic acid. Atty. Dkt: RDWD-048WO Synthesis of drug-linkers [00454] Preparation of (2S,3S,4S,5R,6S)-6-(5-((5S,8S,11S,12R)-11-((S)-sec-butyl)-12-(2- ((S)-2-((1R,2R)-3-(((1S,2R)-1-hydroxy-1-phenylpropan-2-yl)amino)-1-methoxy-2-methyl-3- oxopropyl)pyrrolidin-1-yl)-2-oxoethyl)-5,8-diisopropyl-4,10-dimethyl-3,6,9-trioxo-2,13-dioxa- 4,7,10-triazatetradecyl)-2-((2S,5S,18R)-22-(2-((1,2-dimethylhydrazineyl)methyl)-1H-pyrrolo[2,3- b]pyridin-1-yl)-5-isopropyl-2-methyl-4,7,17,20-tetraoxo-18-(sulfomethyl)-10,13-dioxa- 3,6,16,19-tetraazadocosanamido)phenoxy)-3,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid (5) DMF, and 0.35 mL of DIPEA (2.0 mmol) were combined at room temperature in a 20 mL glass. The resulting mixture was stirred and treated with PNP carbonate 1 (1014 mg, 1.0 mmol) as a solid in a few small portions, followed by the addition of HOAt (136 mg, 1.0 mmol) in one portion at room temperature. Reaction mixture was stirred for 6 h until reaction was judged complete (HPLC). Reaction mixture was poured into 30 mL of water, and the resulting white precipitate was separated and collected, washed with 5 mL of water, and dried briefly under high vacuum to give 1.87 g of crude coupling product as a yellow solid, which was taken to the next step without purification. Atty. Dkt: RDWD-048WO [00456] A solution of crude intermediate (1.87 g) in 15 mL of THF was cooled down to 0°C in an ice bath and treated slowly with 1 M aqueous lithium hydroxide solution (3 mL). Reaction mixture was stirred at 0°C for 3 hours, then warmed up to ambient temperature, treated with 3 mL of 1 M aqueous lithium hydroxide and diluted with 3 mL of methanol. The resulting mixture was stirred at room temperature for 3 hours until hydrolysis was found complete (HPLC), then quenched by adding 1 M aqueous HCl solution to pH 7. Reaction mixture was then concentrated under reduced pressure and washed with 10 mL of MTBE. Aqueous layer was purified by reversed-phase chromatography (C18 column, 0-40% acetonitrile-water with 0.05% TFA). Pure product fractions were combined, concentrated under reduced pressure, and lyophilized to give compound 3 as a white powder (735 mg, 0.60 mmol, 60% yield over 2 steps). LRMS (ESI): m/z 1229.7 [M+H]+, Calculated for C61H96N8O18 m/z 1229.7. [00457] To a stirred solution of compound 3 (735 mg, 0.60 mmol) in 3 mL of anhydrous DMA were added DIPEA (0.21 mL, 1.2 mmol) and a solution of PFP-ester 4 (575 mg, 0.60 mmol) in 2 mL of DMA at room temperature, followed by the addition of HOAt (84 mg, 0.60 mmol). The resulting mixture was stirred for 30 minutes until coupling was judged complete (HPLC analysis), then treated directly with 1.2 mL of piperidine at room temperature. After 15 minutes, reaction mixture was purified by reversed-phase chromatography (C18 column, 0- 40% gradient of acetonitrile-water, no acid additive). Pure fractions were combined, concentrated under reduced pressure to ~ 50 mL final volume, and lyophilized to give compound 5 (808 mg, 0.45 mmol, 75% yield) as a white fluffy powder. LRMS (ESI): m/z 1783.9 [M+H]⁺, Calculated for C84H130N14O26S m/z 1783.9. Synthesis of Compound 4 (1.23 g, 6.68 mmol) in 6.5 mL of anhydrous DMF. This mixture was treated with EDCI-HCl (0.64 g, 3.34 mmol) in one portion at room temperature and stirred for 20 h until 6 was fully consumed as judged by HPLC analysis. Reaction mixture was loaded onto a C18 column and Atty. Dkt: RDWD-048WO eluted with 0-80% gradient of acetonitrile-water with 0.05% TFA additive. Pure fractions were combined, concentrated under reduced pressure until slightly murky, and lyophilized to give PFP-ester product 4 (1.40 g, 1.46 mmol, 87% yield) as a tan powder. LRMS (ESI): m/z 961.2 [M+H]⁺, Calculated for C₄₄H₄₅F₅N₆O₁₁S m/z 961.3. [00459] Preparation of (2S,3S,4S,5R,6S)-6-(2-((28S,31S,34S)-28-(4-(3-(5-((S)-28-(((S)-1- (((S)-1-((2-(((2S,3R,4S,5S,6S)-6-carboxy-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl)oxy)-4-((((2- ((S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2- b]quinolin-11-yl)ethyl)(isopropyl)carbamoyl)oxy)methyl)phenyl)amino)-1-oxopropan-2- yl)amino)-3-methyl-1-oxobutan-2-yl)carbamoyl)-26,34-dioxo-2,5,8,11,14,17,20,23-octaoxa- 27,33-diazaheptatriacontan-37-amido)-2-((1,2-dimethylhydrazineyl)methyl)-1H-indol-1- yl)propanamido)butyl)-31-isopropyl-34-methyl-26,29,32-trioxo-2,5,8,11,14,17,20,23-octaoxa- 27,30,33-triazapentatriacontan-35-amido)-5-((((2-((S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14- tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-11- yl)ethyl)(isopropyl)carbamoyl)oxy)methyl)phenoxy)-3,4,5-trihydroxytetrahydro-2H-pyran-2- carboxylic acid (15)

Atty. Dkt: RDWD-048WO mL of anhydrous DMF and 1.75 mL of DIPEA (10 mmol). The resulting mixture was stirred and treated with HOAt (0.68 g, 5 mmol), followed by PNP-carbonate 1 (5.1 g, 5 mmol) in a few small portions at room temperature. Reaction mixture was stirred at RT for 8 hours until starting materials were judged fully consumed based on HPLC analysis. The mixture was poured onto 300 mL of ice with vigorous stirring, the resulting yellowish precipitate was collected by filtration, washed with 30 mL of cold water twice, dried on air overnight to give 6.7 g of crude coupling product as a light-yellow powder which was taken to the next step without purification. Atty. Dkt: RDWD-048WO [00461] A solution of crude coupling intermediate (6.7 g) in 30 mL of THF was cooled down to 0 °C in an ice bath and treated slowly with 2 M aqueous lithium hydroxide solution (10 mL). Reaction mixture was stirred at 0 °C for 1 hour, then another 10 mL of 2 M LiOH solution was added and stirring continued for 15 minutes before warming the reaction mixture to room temperature and adding another 10 mL of 2 M lithium hydroxide. The resulting mixture was stirred for 1 hour at room temperature, then quenched by adding 2 M aqueous HCl solution to pH ~2-3 and let stir for 30 minutes. The mixture was transferred to a separatory funnel and washed with MTBE (2 x 50 mL). Aqueous layer was separated, then directly loaded on a C18 column, and eluted with 0-40% CH3CN-H2O with 0.05% TFA. Pure fractions were combined, concentrated under reduced pressure to ~70 mL volume, and lyophilized to give 3.4 g of compound 8 (3.6 mmol, 72% yield over 2 steps) as a bright-yellow fluffy powder. LRMS (ESI): m/z 945.4 [M+H]⁺, Calculated for C47H56N6O15 m/z 945.4. [00462] To a stirred mixture of compound 8 (945 mg, 1.0 mmol) and DIPEA (0.35 mL, 2 mmol) in 4 mL DMF were added Boc-Lys(Fmoc)-OPfp 9 (635 mg, 1 mmol) in one portion at room temperature. The resulting turbid mixture was stirred for 30 minutes until it became a clear yellow solution, while the reaction was judged complete by LCMS analysis. Reaction mixture was poured into 50 mL of 10% aq. citric acid solution and extracted with ethyl acetate (2x100 mL). Organic layer was washed once with brine, dried over sodium sulfate, and concentrated under vacuum. The residue was purified by silica gel chromatography using 5- 10% MeOH in DCM as an eluent. Solvents removed under vacuum to give 1.15 g (0.82 mmol, 82% yield) of product 10 as a bright yellow solid. LRMS (ESI): m/z 1395.6 [M+H]⁺, Calculated for C73H86N8O20 m/z 1395.6. [00463] To a stirred solution of compound 10 (1.15 g, 0.82 mmol) in 5 mL of anhydrous DCM were added 5 mL of TFA at RT. Reaction mixture was stirred for 15 minutes, monitored for completion by LCMS. Solvents were immediately removed under reduced pressure, the dark oily residue was briefly dried under high vacuum and triturated with 25 mL MTBE. The resulting light-yellow precipitate was collected by filtration, transferred to a round-bottom Atty. Dkt: RDWD-048WO flask, and dried under high vacuum overnight to give 1.2 g of crude product 11 as light-yellow powder (TFA salt). LRMS (ESI): m/z 1295.5 [M+H]⁺, Calculated for C₆₈H₇₈N₈O₁₈ m/z 1295.6. [00464] To a solution of mPEG8 acid (340 mg, 0.82 mmol) in 5 mL of anhydrous THF were added pentafluorophenol (180 mg, 0.98 mmol), followed by DCC (170 mg, 0.82 mmol) at room temperature. The resulting mixture was stirred overnight, solids were filtered off, and washed with THF on filter. Combined filtrate was concentrated under reduced pressure, to give crude compound 12 (clear oil), which was re-dissolved in 2 mL of DMF and combined with a stirred mixture of crude compound 11 (0.82 mmol) and DIPEA (0.43 mL, 2.5 mmol) in 4 mL of DMF. Reaction mixture was stirred for 1 hour at room temperature until judged complete by HPLC analysis based on consumption of 11. Reaction mixture was directly treated with 3 mL of triethylamine and stirring continued at room temperature for 7 hours until Fmoc-deprotection was complete based on HPLC analysis. Triethylamine and partially DMF were removed under reduced pressure, and the residual mixture was purified by reversed-phase chromatography (C18 column 0-40% CH3CN-H2O with 0.05% TFA). Pure fractions were combined, concentrated under reduced pressure to ~70 mL final volume, and lyophilized to give 932 mg of product 13 as a bright-yellow light powder (0.64 mmol, 78% yield over 3 steps starting from 10). LRMS (ESI): m/z 1467.7 [M+H]⁺, Calculated for C71H102N8O25 m/z 1467.7. [00465] To a stirred solution of compound 13 (3.5 g, 2.4 mmol) in 16 mL of anhydrous DMA were added DIPEA (0.84 mL, 4.8 mmol) and HOAt (0.33 g, 2.4 mmol) at room temperature. The resulting mixture was treated with a separately prepared solution of bis-PFP- ester 14 (1.0 g, 1.1 mmol in 4 mL of DMA) in small portions (2 mL, 1 mL, 0.75 mL, and 0.5 mL) with 10 minutes intervals between additions. After the addition was complete, reaction mixture was stirred for 15 minutes at room temperature and treated with 2.1 mL of piperidine (22 mmol). After 20 minutes, reaction mixture was directly purified by reversed-phase chromatography (C18 column, 0-40% CH3CN-H2O with 0.05% TFA). Pure fractions were combined, concentrated under reduced pressure to ~100 mL final volume, and lyophilized to obtain 3.2 g of compound 15 as a bright-yellow fluffy powder (0.98 mmol, 89% yield for two steps based on 14). LRMS (ESI): m/z 1638.3 [M+H]²⁺, Calculated for C₁₆₀H₂₂₄N₂₀O₅₃ m/z 1638.8. Atty. Dkt: RDWD-048WO [00466] Synthesis of Boc-Lys(Fmoc)-OPfp 9. [00467] To a stirred solution of Boc-Lys(Fmoc)-OH (4.7 g, 10 mmol) in 40 mL of anhydrous THF were added pentafluorophenol (2.2 g, 12 mmol), followed by DCC (2.1 g, 10 mmol) in small portions at room temperature. The resulting mixture was stirred overnight, solids were filtered off, washed with THF on filter. Combined filtrate was concentrated under vacuum, and the white solid residue was triturated with DCM-EtOAc mixture, collected by filtration, and dried under vacuum to give 4.9 g (7.8 mmol, 78% yield) of Boc-Lys(Fmoc)-OPfp 9 as a white powder. LRMS (ESI): m/z 657.3 [M+Na]⁺, Calculated for C₃₂H₃₁F₅N₂O₆ m/z 657.2. [00468] A solution of bis-acid 16 (2.0 g, 3.34 mmol) in 40 mL of anhydrous THF was combined with 6.2 g (33.4 mmol) of pentafluorophenol. The mixture was stirred and treated with DCC (2.0 g, 10 mmol) in a few small portions at room temperature. Reaction mixture was stirred for 48 hours at RT, then all solids were removed by filtration and washed with THF on filter. Combined filtrates were concentrated under vacuum and purified by silica gel chromatography (0-25-35% gradient of EtOAc-Hexanes) to give 2.4 g of bis-PFP ester 14 (2.6 mmol, 77% yield) as a white foaming solid. LRMS (ESI): m/z 931.2 [M+H]⁺, Calculated for C45H32F10N4O7 m/z 931.2. [00469] Preparation of (2S,5S,18R)-1-((4-((5S,8S,11S,12R)-11-((S)-sec-butyl)-12-(2-((S)-2- ((1R,2R)-3-(((1S,2R)-1-hydroxy-1-phenylpropan-2-yl)amino)-1-methoxy-2-methyl-3- oxopropyl)pyrrolidin-1-yl)-2-oxoethyl)-5,8-diisopropyl-4,10-dimethyl-3,6,9-trioxo-2,13-dioxa- 4,7,10-triazatetradecyl)-2-hydroxyphenyl)amino)-18-(3-(2-((1,2-dimethylhydrazineyl)methyl)- 1H-pyrrolo[2,3-b]pyridin-1-yl)propanamido)-5-isopropyl-2-methyl-1,4,7,17-tetraoxo-10,13- dioxa-3,6,16-triazanonadecane-19-sulfonic acid (25).

Atty. Dkt: RDWD-048WO 25 mL of anhydrous THF were added triethylamine (2.5 mL, 18 mmol), followed by acetyl chloride (1.1 mL, 15 mmol) at ambient temperature. Reaction mixture was allowed to stir for 30 min, quenched with water (20 mL), and extracted with DCM. Combined organic layer was washed with water and brine, dried over Na₂SO_4, and concentrated under vacuum to give 2.6 g of crude product 18 as a pale yellow solid, which was used in the next step without purification. [00471] Crude compound 18 (400 mg) was suspended in a mixture of MeOH: EtOAc (1: 3, 10 mL), treated with palladium on carbon (10 wt. %, 400 mg) and stirred overnight under hydrogen atmosphere. Reaction mixture was then filtered through a pad of Celite and concentrated under vacuum. The residue was purified by silica gel chromatography using 10% MeOH in DCM as an eluent to give 275 mg of compound 19 as a yellowish orange solid. [00472] To a stirred solution of Fmoc-Val-Ala-OH 20 (350 mg, 0.86 mmol) in anhydrous DMF (5 mL) were added HATU (480 mg, 1.25 mmol) and DIPEA (0.58 mL, 3.3 mmol). The Atty. Dkt: RDWD-048WO resulting mixture was stirred for 30 min and combined with compound 19 (200 mg, 1.1 mmol). After 1 h, reaction was quenched with sat. NH₄Cl, transferred to a separatory funnel and extracted with EtOAc. Organic layer was washed with water and brine, dried over Na₂SO₄, filtered, and concentrated under vacuum. The residue was purified by silica gel chromatography using 10% MeOH in DCM as an eluent to afford compound 21 (305 mg, 0.53 mmol, 61% yield) as a pale yellow solid. LRMS (ESI): m/z 574.3 [M+H]⁺, Calculated for C₃₂H₃₅N₃O₇ m/z 574.3. [00473] To a solution of compound 21 (350 mg, 0.61 mmol) in anhydrous DMF (10 mL) were added bis-(p-nitrophenyl) carbonate (280 mg, 0.92 mmol) and DIPEA (1.0 mL, 5.7 mmol) at room temperature. Reaction mixture was stirred for 1 h, quenched with sat. aqueous NH4Cl and extracted with EtOAc. Combined organic layer was washed with water and brine, dried over Na2SO4, filtered, and concentrated in vacuum. The residue was purified by silica gel chromatography using 10% MeOH in as an eluent to give 400 mg (0.54 mmol, 89 % yield) of PNP-carbonate 22 as an off-white solid. LRMS (ESI): m/z 739.2 [M+H]⁺, Calculated for C39H38N4O11 m/z 739.3. [00474] In a 20 mL scintillation vial were combined MMAE 2 (52 mg, 72 μmol) and PNP- carbonate 22 (50 mg, 72 μmol) in 3 mL of anhydrous DMF, followed by DIPEA (60 μL, 0.34 mmol) and HOAt (12 mg, 72 μmol) at room temperature. Reaction mixture was stirred for 4 h, quenched with 10% aq. TFA solution (10 mL), extracted with DCM. Organic layer was washed with water and brine, dried over sodium sulfate. Solvent was removed in vacuum and the residue was purified by silica gel chromatography (0-10% MeOH in DCM gradient) to give 75 mg (57 μmol, 79 % yield) of compound 23 as a white solid. LRMS (ESI): m/z 1317.7 [M+H]⁺, Calculated for C72H100N8O15 m/z 1317.7. [00475] Compound 23 (75 mg, 57 μmol) was dissolved in MeOH (4 mL) and 0.5 mL of water and treated with K2CO3 (80 mg, 0.58 mmol) at room temperature. The mixture was stirred for 1 h, quenched with 1 % aqueous solution of TFA (5 mL) and directly purified by reversed-phase prep HPLC (C18 column, 0 - 50 % acetonitrile-water/0.05% TFA as gradient). Pure fractions were combined and lyophilized to give 7.5 mg of compound 24 as a white solid (7 μmol, 12 % yield). LRMS (ESI): m/z 1052.7 [M+H]⁺, Calculated for C₅₅H₈₈N₈O₁₂ m/z 1052.6. Atty. Dkt: RDWD-048WO [00476] To a stirred solution of compound 24 (7.5 mg, 7 μmol) in anhydrous DMF (2.0 mL) were added Pfp-ester 4 (8 mg, 7 μmol), followed by HOAt (1.5 mg, 11 μmol) and DIPEA (10 μL, 57 μmol) at room temperature. Reaction mixture was stirred for 1 h, and then directly treated with piperidine (14 μL, 0.14 mmol). After 20 min, the mixture was purified by reversed- phase prep HPLC (C18 column, 0 - 50 % acetonitrile-water/0.05% TFA as gradient). Pure fractions were combined and lyophilized to give 8 mg (5 μmol, 71% yield) of compound 25 as a white solid. LRMS (ESI): m/z 1607.8 [M+H]⁺, Calculated for C₇₈H₁₂₂N₁₄O₂₀S m/z 1607.9. [00477] Synthesis of construct 29 4-azanonadecan-19-oate (27) [00479] In an oven-dried scintillation vial were combined 1-(9H-fluoren-9-yl)-3-oxo- 2,7,10,13,16-pentaoxa-4-azanonadecan-19-oic acid (26, 487 mg, 1 mmol) and pentafluorophenol (368 mg, 2 mmol) in 5 mL of anhydrous THF. The resulting mixture was treated with DCC (247 mg, 1.2 mmol) in one portion at room temperature, and reaction mixture was stirred overnight. Precipitated solids were filtered off, solvents removed under vacuum, and the residue was purified by reversed-phase chromatography (C18 column, 10- 100% v/v gradient of CH₃CN/H₂O with 0.05% TFA) to give 670 mg of PFP ester 27 (570 mg, 0.87 mmol, 87% yield) as a colorless oil. LRMS (ESI): m/z 654.2 [M+H]⁺, Calculated for C₃₂H₃₂F₅NO₈ m/z 654.2. Atty. Dkt: RDWD-048WO [00480] Preparation of (2S,3S,4S,5R,6S)-6-(2-((17S,20S)-1-amino-17-isopropyl-20-methyl- 15,18-dioxo-3,6,9,12-tetraoxa-16,19-diazahenicosan-21-amido)-5-((((2-((S)-4-ethyl-4-hydroxy- 3,14-dioxo-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-11- yl)ethyl)(isopropyl)carbamoyl)oxy)methyl)phenoxy)-3,4,5-trihydroxytetrahydro-2H-pyran-2- carboxylic acid (28) [00481] Compound 8 (262 mg, 0.22 mmol) was dissolved in 4 mL of DMF. To this solution were added DIPEA (105 µL, 0.66 mmol) and PFP ester 27 (181 mg, 0.22 mmol) as a solution in 0.5 mL of DMF, followed by HOAt (38 mg, 0.22 mmol). The resulting mixture was allowed to stand at room temperature for one hour, then treated directly with 4 mL of triethylamine. Reaction mixture was stirred for 5 hours, until Fmoc-deprotection was complete as judged by LCMS analysis. Reaction mixture was concentrated under vacuum and purified by reversed-phase chromatography (C18 column, 0-50% v/v gradient of CH3CN/H2O with 0.05% TFA) to give 185 mg (0.16 mmol, 73% yield) of compound 28 as a yellow powder. LRMS (ESI): m/z 1192.5 [M+H]⁺, Calculated for C58H77N7O2 m/z 1192.5. [00482] Preparation of (2S,3S,4S,5R,6S)-6-(2-((2S,5S)-25-(5-((2S,5S)-1-((2- (((2S,3R,4S,5S,6S)-6-carboxy-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl)oxy)-4-((((2-((S)-4-ethyl- 4-hydroxy-3,14-dioxo-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-11- yl)ethyl)(isopropyl)carbamoyl)oxy)methyl)phenyl)amino)-5-isopropyl-2-methyl-1,4,7,23- tetraoxo-10,13,16,19-tetraoxa-3,6,22-triazahexacosan-26-amido)-2-((1,2- dimethylhydrazinyl)methyl)-1H-indol-1-yl)-5-isopropyl-2-methyl-4,7,23-trioxo-10,13,16,19- tetraoxa-3,6,22-triazapentacosanamido)-5-((((2-((S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14- tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-11- yl)ethyl)(isopropyl)carbamoyl)oxy)methyl)phenoxy)-3,4,5-trihydroxytetrahydro-2H-pyran-2- carboxylic acid (29) [00483] Compound 28 (23 mg, 19 µmol) was dissolved in 2 mL of anhydrous DMA. To this solution were added DIPEA (10 µL, 57 µmol) and bis-PFP ester 14 (8 mg, 8.6 µmol) as solid in one portion at room temperature, followed by HOAt (2.6 mg, 19 µmol). The resulting mixture was allowed to stand at room temperature for one hour, then treated directly with 17 Atty. Dkt: RDWD-048WO µL of piperidine (172 µmol). After 20 minutes, reaction mixture was purified by reversed- phase chromatography HPLC (C18 column, 0-50% v/v gradient of CH₃CN/H₂O with 0.05% TFA). Pure fractions were lyophilized to give 5.8 mg (2.1 µmol, 24 % yield) of compound 29 as a yellow powder. LRMS (ESI): m/z 1363.1 [M+2H]⁺⁺, Calculated for C₁₃₄H₁₇₄N₁₈O₄₃ m/z 1362.6. [00484] Preparation of (2S,3S,4S,5R,6S)-6-(2-((S)-2-((S)-2-(4-((1-(3-(((S)-1-(((S)-1-((4- ((5S,8S,11S,12R)-11-((S)-sec-butyl)-12-(2-((S)-2-((1R,2R)-3-(((1S,2R)-1-hydroxy-1-phenylpropan- 2-yl)amino)-1-methoxy-2-methyl-3-oxopropyl)pyrrolidin-1-yl)-2-oxoethyl)-5,8-diisopropyl-4,10- dimethyl-3,6,9-trioxo-2,13-dioxa-4,7,10-triazatetradecyl)-2-(((2S,3R,4S,5S,6S)-6-carboxy-3,4,5- trihydroxytetrahydro-2H-pyran-2-yl)oxy)phenyl)amino)-1-oxopropan-2-yl)amino)-3-methyl-1- oxobutan-2-yl)amino)-3-oxopropyl)-2-((1,2-dimethylhydrazinyl)methyl)-1H-indol-5-yl)amino)-4- oxobutanamido)-3-methylbutanamido)propanamido)-5-((5S,8S,11S,12R)-11-((S)-sec-butyl)-12- (2-((S)-2-((1R,2R)-3-(((1S,2R)-1-hydroxy-1-phenylpropan-2-yl)amino)-1-methoxy-2-methyl-3- oxopropyl)pyrrolidin-1-yl)-2-oxoethyl)-5,8-diisopropyl-4,10-dimethyl-3,6,9-trioxo-2,13-dioxa- 4,7,10-triazatetradecyl)phenoxy)-3,4,5-trihydroxytetrahydro-2H-pyran-2-carboxylic acid (30) and 2 mL of anhydrous DMA, followed by 15 µL of DIPEA (84 µmol) and 4 mg of HOAt (28 µmol). The resulting mixture was treated with bis-PFP ester 14 (13 mg, 14 µmmol) as a solid in Atty. Dkt: RDWD-048WO portion at room temperature, and let stir for 3 hours, until starting materials were fully consumed as judged by LCMS analysis. Reaction mixture was directly treated with 56 µL (0.56 mmol) of piperidine at room temperature, let stand for 20 minutes, and purified by reversed- phase HPLC (C18, 0-75% v/v CH3CN-H2O with 0.05% TFA). Lyophilized pure fractions gave 21 mg of compound 30 (7.5 µmol, 54 % yield) as a white powder. LRMS (ESI): m/z 1400.3 [M+2H]⁺⁺, Calculated for C₁₄₀H₂₁₂N₂₀O₃₉ m/z 1399.8. [00486] The structures of drug-linkers 31 and 32 are shown below. Compound 31 was previously described in the PCT Publication WO 2019/113248; the synthesis of compounds 32 was reported in PCT Publication WO 2015/081282. Both these publications are incorporated by reference in their entirety. [00487] Synthesis of azide intermediate 36 Atty. Dkt: RDWD-048WO [00488] To a stirred solution of compound 33 (907 mg, 1.16 mmol) in 2 mL of anhydrous DMF were added DIPEA (0.60 mL, 3.4 mmol), followed by HATU (443 mg, 1.16 mmol) at room temperature. The resulting mixture was stirred for 30 min and then combined with a solution of compound 8 (1.0 g, 1.06 mmol) in 4 mL of DMF. After 1 h, reaction mixture was treated with 1.2 mL of triethylamine, stirred at RT for 5 h, until Fmoc-deprotection was judged complete by LCMS analysis. Reaction mixture was concentrated under reduced pressure to remove triethylamine and partly DMF, and the residue was purified by reversed-phase chromatography (C18, 0-40% acetonitrile-water/0.05% TFA). Pure fractions were combined and lyophilized to give 800 mg of compound 34 (0.54 mmol, 51% yield over two steps) as a light-yellow powder. LRMS (ESI): m/z 1483.6 [M+H]⁺, Calcd for C71H102N8O26 m/z 1483.7. [00489] To a stirred solution of compound 34 (287 mg, 0.19 mmol) in 2 mL of anhydrous DMA were added DIPEA (0.10 mL, 0.57 mmol), followed by PFP-ester 35 (73 mg, 0.19 mmol) in one portion at room temperature. Reaction mixture was stirred for 30 min, then directly purified by reversed-phase chromatography (C18, 0-40% acetonitrile-water/0.05% TFA). Pure fractions were combined, concentrated in vacuum, and lyophilized to give 220 mg of compound 36 (0.13 mmol, 68% yield) as a light-yellow powder. LRMS (ESI): m/z 1676.7 [M+H]⁺, Calcd for C81H113N9O29 m/z 1676.8. [00490] Synthesis of Pfp-ester 35 was combined with pentafluorophenol (555 mg, 3 mmol) in 4 mL of anhydrous THF. The resulting mixture was treated with DCC (622 mg, 3 mmol) at RT. Reaction mixture was stirred overnight, then solids were removed by filtration, the filtrate was concentrated and purified by silica gel chromatography using 0-40% EtOAc/Hexanes to give 150 mg of compound 35 (0.2 mmol, 67% yield) as a brownish solid. LRMS (ESI): m/z 762.2 [M+H]⁺, Calcd for C₃₈H₃₂F₅N₇O₅ m/z 762.2. Atty. Dkt: RDWD-048WO [00492] Synthesis of iRGD-alkyne 41 DMF, treated with DIPEA (25 µL, 150 µmol), followed by a solution of Pfp ester 39 (33 mg, 48 µmol) in 0.5 mL of DMF. Reaction mixture was allowed to stir at RT for 2 h, until reaction was judged complete by LCMS analysis. Reaction mixture was directly purified by reversed-phase chromatography (C18, 0-35% acetonitrile-water, 0.05% TFA). Fractions containing product were combined, solvent removed using rotovap, and the residue was kept under high vacuum overnight to obtain 54 mg of product 40 as a white solid. The solid was then dissolved in 2 mL of formic acid and stirred for 20 minutes. Formic acid was then removed under vacuum to obtain 50 mg of compound 41 as a colorless solid (34 µmol, 71 % yield). LRMS (ESI): m/z 1451.6 [M+H]⁺, Calcd for C59H98N14O24S2 m/z 1451.6. Atty. Dkt: RDWD-048WO [00494] Synthesis of linker 39 DMF, treated with DIPEA (0.25 mL), followed by HATU (183 mg, 0.48 mmol) at RT. The resulting mixture was stirred for 15 min and combined with a solution of compound 44 (240 mg, 0.48 mmol) in 1 mL of DMF. After 30 min, reaction mixture was purified by reversed-phase chromatography (C18, 0-50% acetonitrile-water, 0.05 % TFA gradient). Pure fractions were combined, concentrated on rotovap, and the residue was dried under high vacuum overnight to give 244 mg of compound 46 as a clear yellowish oil (0.42 mmol, 88 % yield). LRMS (ESI): m/z 595.4 [M+Na]⁺, Calcd for C28H51NO11 m/z 595.4. [00496] Compound 46 (244 mg, 0.42 mmol) was dissolved in a mixture of TFA (2 mL), DCM (2 mL) and 0.5 mL of triisopropylsilane at RT. After 30 min, deprotection was judged complete by LCMS analysis. Reaction mixture was concentrated under reduced pressure; the residue was dissolved in DMF and purified by reversed-phase chromatography (C18, 0-50% acetonitrile-water, 0.05 % TFA). Pure fractions were concentrated and dried under high vacuum overnight to give 210 mg of compound 47 (0.40 mmol, 95% yield). LRMS (ESI): m/z 522.3 [M+H]⁺, Calcd for C₂₄H₄₃NO₁₁ m/z 522.3. [00497] Carboxylic acid 47 (210 mg, 0.40 mmol) was dissolved in 4 mL of anhydrous DCM and treated with pyridine (1 mL), followed by pentafluorophenol trifluoroacetate 48 (1 mL) at RT. The resulting mixture was stirred for 1 h, then volatiles were removed under vacuum, and the residue was purified by reversed-phase chromatography (C18, 0-70% acetonitrile-water, 0.05 % TFA). Pure fractions were combined and concentrated under vacuum. The resulting colorless oil was dried under vacuum overnight to give 255 mg of Pfp- ester 39 (0.37 mmol, 93 % yield). LRMS (ESI): m/z 688.3 [M+H]⁺, Calcd for C₃₀H₄₂F₅NO₁₁ m/z 688.3. Atty. Dkt: RDWD-048WO [00498] Preparation of 2,2'-((3S,6R,11R,14S,20S,23S,31aS)-23-(4-aminobutyl)-6- carboxy-11-(1-(1-(3-((1-((S)-29-(((S)-1-(((S)-1-((2-(((2S,3R,4S,5S,6S)-6-carboxy-3,4,5- trihydroxytetrahydro-2H-pyran-2-yl)oxy)-4-((((2-((S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14- tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-11- yl)ethyl)(isopropyl)carbamoyl)oxy)methyl)phenyl)amino)-1-oxopropan-2-yl)amino)-3-methyl-1- oxobutan-2-yl)carbamoyl)-27,35-dioxo-2,5,8,11,14,17,20,23,26-nonaoxa-28,34- diazaheptatriacontan-37-yl)-2-((1,2-dimethylhydrazineyl)methyl)-1H-indol-5-yl)amino)-3- oxopropyl)-1H-1,2,3-triazol-4-yl)-3-oxo-7,10,13,16,19,22,25,28-octaoxa-4-azahentriacontan- 31-amido)-14-(3-guanidinopropyl)-1,4,12,15,18,21,24,27-octaoxooctacosahydro-1H- pyrrolo[2,1-j][1,2]dithia[5,8,11,14,17,20,23,26]octaazacyclononacosine-3,20-diyl)diacetic acid (43)

Atty. Dkt: RDWD-048WO

Atty. Dkt: RDWD-048WO [00499] Azide 36 (28 mg, 13.5 µmol), alkyne 41 (20 mg, 13.5 µmol) and 35 µL of aqueous CuSO4 solution (0.1 M, 2.7 µmol) were combined in 2 mL of tert-butanol-water mixture (1:1 v/v). Reaction vessel was sealed, degassed under vacuum, and backfilled with nitrogen. Reaction mixture was then treated with sodium ascorbate solution (100 µmol of 0.1 M in water, 10 µmol) at RT under nitrogen and allowed to stir for 2 h, until reaction was judged complete by LCMS analysis. Solvents were removed in vacuum, and the residue was purified by reversed-phase prep HPLC (30 mm C18, 0-60% CH₃CN/water, 0.05% TFA. Combined pure fractions were concentrated on rotovap and lyophilized to give 21 mg of compound 42 as a yellowish powder (6 µmol, 44% yield). LRMS (ESI): m/z 1757.0 [M+2H]⁺⁺, Calcd for C162H231N29O54S2 m/z 1757.3. [00500] To a solution of compound 42 (21 mg, 6 µmol) in 2 mL of DMA were added piperidine (12 µL, 120 µmol) at RT. Reaction mixture was stirred for 20 minutes and purified by reversed-phase prep HPLC (C1821 mm, 0-40% CH3CN/water, 0.05% TFA). Combined pure fractions and directly lyophilized to obtain 13.5 mg of compound 43 as a yellowish solid (4 µmol, 68 % yield). LRMS (ESI): m/z 1645.8 [M+2H]⁺⁺, Calcd for C147H221N29O52S2 m/z 1645.6. Example 2 – Preparing and Testing Double and Triple Tag Antibody conjugates Method: Triple Tag Conjugation Protocol with Compound 15: [00501] An antibody (Final concentration = 15 mg/mL) bearing three aldehyde tags was conjugated to Compound 15 for 72 h at 37 deg C in 20/50 buffer with 2.00 mM drug linker and 50 mM of sodium citrate from a stock solution of 500 mM sodium citrate at pH = 5.5. The antibody stock solution was 20 mg/mL in 20/50 buffer at pH 5.5. The Compound 15 drug linker stock solution was 50 mM in DMA. After conjugation, free drug was removed using a 30 kD MWCO 0.5 mL Amicon spin concentrator. Samples were added to the spin concentrator, centrifuged at 15,000 x g for 7 min, then diluted with 450 mL 20 mM sodium citrate, 50 mM NaCl pH 5.5 (20/50 buffer), and centrifuged again. The process was repeated 10 times. To determine the drug-antibody ratio (DAR) of the intermediate product, antibody-drug conjugates (ADCs) were examined by analytical chromatography using HIC (Tosoh #14947) or PLRP-RP (Agilent PL1912-18021000A, 8 mm, 50 x 2.1 mm) columns. HIC analysis used mobile phase A: 1.5 M ammonium sulfate, 25 mM sodium phosphate pH 7.0, and mobile phase B: 25% Atty. Dkt: RDWD-048WO isopropanol, 18.75 mM sodium phosphate pH 7.0. PLRP analysis used mobile phase A: 0.1% trifluoroacetic acid in water, and mobile phase B: 0.1% trifluoroacetic acid in acetonitrile. Prior to PLRP analysis, sample was denatured with the addition of 50 mM DTT, 4 M guanidine HCl (final concentrations) and heating at 37°C for 30 min. To determine aggregation, samples were analyzed using analytical size exclusion chromatography (SEC; Tosoh #08541) with a mobile phase of 300 mM NaCl, 25 mM sodium phosphate pH 6.8 with 5% isopropanol. Method: Triple Tagged Conjugation Protocol with Compound 5 [00502] To produce triple tagged conjugates, an aldehyde-tagged antibody (Final concentration = 15 mg/mL) in 20 mM sodium citrate, 50 mM NaCl pH 5.5 (20/50 buffer) buffer was reacted with compound 5 at 2.55 mM. The compound 5 drug linker stock solution was in 50 mM DMA. The reaction proceeded for 72 h at 37 deg C in 20/50 buffer and 50 mM of sodium citrate from a stock solution of 500 mM sodium citrate at pH=5.5. After conjugation, free drug was removed using a 0.5-mL Amicon spin filter with a 30 kD MWCO. Samples were added to the spin concentrator, centrifuged at 14,000 x g for 7 min, then diluted with 450 mL 20 mM sodium citrate, 50 mM NaCl pH 5.5 (20/50 buffer), and centrifuged again. The process was repeated 10 times. To determine the drug-antibody ratio (DAR) of the intermediate product, antibody-drug conjugates (ADCs) were examined by analytical chromatography using PLRP-RP (Agilent PL1912-18021000A, 8 mm, 50 x 2.1 mm) columns. PLRP analysis used mobile phase A: 0.1% trifluoroacetic acid in water, and mobile phase B: 0.1% trifluoroacetic acid in acetonitrile. Prior to PLRP analysis, sample was denatured with the addition of 50 mM DTT, 4 M guanidine HCl (final concentrations) and incubated at 37°C for 30 min. To determine aggregation, samples were analyzed using analytical size exclusion chromatography (SEC; Tosoh #08541) with a mobile phase of 300 mM NaCl, 25 mM sodium phosphate pH 6.8 with 5% isopropanol. [00503] Experimental Results: Adding more than two tag sites into an antibody and expecting to generate a manufacturable protein and conjugate (e.g., ADC) seemed like an unreasonable and unreachable goal. Accordingly, a triple tagged antibody was first produced by accident, where a single-tagged light chain was co-expressed with double-tagged heavy chain variants, which produced triple-tagged trastuzumab antibodies (Table 6). Antibody titers Atty. Dkt: RDWD-048WO were desirable. Also, when conjugates (with Compound 5) were made and analyzed, the conjugated light chain was observed along with the doubly-conjugated heavy chains. Moreover, several of the triple-tag combinations produced ADCs with DARs of > 5 and low levels (< 5%) of high molecular weight species, i.e., antibody aggregates. Thus, these triple- tagged antibodies provided ADCs with highly-unexpected biophysical and functional properties, which offered the possibility of producing unique molecules with particular functions. [00504] For example, such antibodies could be used where a straight (not branched) linker was desired but a DAR of greater than 4 was needed. Also, they could be used where a branched linker is used, but a DAR higher than 8 was desired. For example, higher DAR conjugates could be useful for targeted delivery of lower-potency payloads, especially non- cytotoxic payloads, such as protein degraders (e.g., thalidomide, lenalidomide, pomalidomide, CC-90009, iberdomide, and mezigdomide), kinase inhibitors, and immunomodulators. Moreover, triple-tagged antibodies could be used where two payloads or cargos were appended to a single, branched linker and the individual DARs of each payload/cargo were desired to be over 4. In each of the envisioned applications for triple-tagged antibodies and their conjugates, different linker-payload combinations are intended. Having access to multiple single tags suitable for use in combination, combinations for conjugate optimization can be made for producing desirable ADCs. [00505] Therefore, to identify additional triple tag combinations suitable for generating various ADCs, promising double tag combinations were used as a base, and a third tag was added to produce triple tag combinations. For example, the CH1/CT tag combination has been used successfully in many contexts to generate manufacturable ADCs (e.g., see Tables 1-5). This double tag combination formed the basis of several triple tag combinations (Table 6). Also, triple tag variations were produced based on tag placements similar to the CH1/CT + light chain tag combination. For example, 58Q/CT base was combined with various light chain tags (Table 7A-7B). [00506] Triple tagged antibodies were also made using only internal tags, avoiding the C- terminal heavy chain tag element, which is the most exposed conjugation site. In the initial triple tag series, both the 22A/116E tag combination and the 22A/58Q tag combination each Atty. Dkt: RDWD-048WO successfully paired with two different third tag sites. Table 7 shows a set of triple tagged antibodies made using only internal tags. Example 3 – Production parameters and properties of double and triple tagged antibodies [00507] Trastuzumab parental antibody modified to contain two tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Table 1 below. %HMW indicates the percentage of high-molecular weight species in the ADC preparations. For example, 1.7% HMW means that the remaining 98.3% is monomer. [00508] Table 1. Double Tag Combinations With Trastuzumab Target Branched %HMW Straight %HMW T 1 T 2 Titer Tag 1 Tag 2 Link r (Br n h d Link r (Str i ht ) Atty. Dkt: RDWD-048WO HER2 ^{CH1 CT} ₃₉₀ 0.7 0.5 6.6 8.43 _{3.81 2.97} HER2 ^{CH1 51S} ₄₇₈ 0.2 0.1 ***straight linker conjugates used Compounds 32, 31, or 5 n/t, not tested [00509] Polatuzumab parental antibodies modified to contain two tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Table 2 below: [00510] Table 2. Double Tag Combinations With Polatuzumab Target Titer Tag 1 Tag 2 Branched %HMW Straight %HMW ht ) Atty. Dkt: RDWD-048WO CD79b 61G CT 775 CD79b CT 51S 378.6 n/t n/t 7.06 0.9 3.65 3.1 branched linker conjugates used Compounds 15 or 30 ***straight linker conjugates used Compounds 32, 31, or 5 n/t, not tested n.d., not determined [00511] Gemtuzumab parental antibodies modified to contain two tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Table 3 below: Atty. Dkt: RDWD-048WO [00512] Table 3. Double Tag Combinations With Gemtuzumab Tag Tag Straight %HMW Branched %HWM Target Tag 1 Tag 2 Titer (Str 1 2 Linker (Branched ti L* Linker aight *** ) Atty. Dkt: RDWD-048WO *bolded titers were less than 25% of the average titer **Straight linker conjugates used Compounds 32, 31, or 5 ***%LMWS indicates the percentage of low-molecular weight species and %HMWS indicates the percentage of high-molecular weight species in the ADC preparation. [00513] Anti-FITC parental antibodies modified to contain two tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Table 4 below: [00514] Table 4. Double Tag Combinations With anti-FITC Target g 2 Tite Branched %HMWS Straight %HMWS Tag 1 Ta r Tag 1 Tag 2 Linker (Branched Linker (Straight ) g g p , , [00515] Numerous parental antibodies modified to contain two tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Table 5 below: [00516] Table 5. Double Tag Combinations With Numerous Antibodies Branched %HMW Straight %HMW ht ) Atty. Dkt: RDWD-048WO S^GN-33a 186V 22A 233.8 6.88 4.52 anti- 186V 22A 6.57 2.44 [00517] Anti-HER2 parental antibody modified to contain three tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Table 4 below: [00518] Table 6. Triple Tag Combinations With anti-HER2 Target T Straight %HMW T 1 T 2 T 3 iter Tag 1 Tag 2 Tag 3 Link r (Str i ht [00519] Numerous parental antibodies modified to contain three tags, each conjugated to a payload were produced. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided in Tables 7A-7B below: [00520] Table 7A. Triple Tag Combinations With Numerous Antibodies (certain parameters) Straight %HMW ht ) Atty. Dkt: RDWD-048WO Her2 CH1 CT 22A 496 0.1 0.2 4.8 5.67 2.6 Her2 CH1 CT 22A 193.7 0.1 0.1 0.3 5.35 1.7 [00521] Table 7B. Triple Tag Combinations With Numerous Antibodies (certain parameters) Branched % HMW Melt Temp 1 Melt Temp Target Linker (Branched (C) 2 (C) * Atty. Dkt: RDWD-048WO [00522] Parental antibodies that bind to Napi2B and Her2 and modified to contain three tags, each conjugated to a payload were produced. The linker used for these conjugations were more hydrophobic straight linkers that lacked the solubilizing glucuronic acid used in Compound 5. The details of various tags are provided elsewhere in this disclosure. Various tested parameters and properties are provided Table 8 below: [00523] Table 8. Triple Tag Combinations With Napi2B and Her2 Antibodies Conjugated via Hydrophobic Straight Linker More % HMW (More Target Tag 1 Tag 2 Tag 3 Titer Tag 1 Tag 2 Tag 3 Hydrophobic Hydrophobic r) Example 4 – Anti-cancer properties of certain triple-tagged ADCs and comparator molecules disclosed herein [00524] Anticancer activities of certain antibody drug conjugates disclosed herein were tested in several cell lines expressing the target antigen. Cell lines were plated in 96-well plates (Costar 3610) at a density of 5 x 10⁴ cells/well in 100 µL of growth media. The next day, cells were treated with 20 μL of test articles serially-diluted in media. After incubation at 37°C with 5% CO₂ for 5 days, viability was measured using the Promega CellTiter Glo® reagent according to the manufacturer’s recommendations. GI50 curves were calculated in GraphPad Prism normalized to the payload concentration. [00525] For example, FIG.1 provides in vitro potency of anti-HER2 MMAE-conjugated ADCs or controls against HER2-positive NCI-N87 cells. Atty. Dkt: RDWD-048WO [00526] Similarly, FIG.2 provides in vitro potency of anti-NaPi2b MMAE-conjugated ADCs or controls against NaPi2b-expressing OVCAR3 cells. [00527] Further, FIG.3 provides in vitro potency of anti-NaPi2b belotecan-conjugated ADCs or controls against NaPi2b-expressing OVCAR3 cells. [00528] Furthermore, FIG.4 provides in vitro potency of anti-HER2 belotecan- conjugated ADCs or controls against HER2-positive NCI-N87 cells. [00529] In all cases, the ADCs were potent against the target cell lines, reducing the % viability by a magnitude similar to that of the free payload (either MMAE or belotecan) or the comparator ADC (single or double-tagged) when dosed at equal concentrations. Example 5 – Biophysical Characterization of Certain Triple-Tagged Antibodies Disclosed Herein [00530] This protocol describes the Affinity-Capture Self-Interaction Nanoparticle Spectroscopy (AC-SINS) assay to monitor the propensity of antibodies to self-associate. [00531] MATERIALS [00532] Goat Anti-human IgG (Jackson ImmunoResearch Lab, 109-005-098) [00533] Goat Non-specific IgG (Jackson ImmunoResearch Lab, 005-000-003) [00534] Amicon 30kDa MWCO Centrifugal Filters (Sigma Aldrich, UFC803096) [00535] 20nm Gold Nanoparticles (Ted Pella, 15705) [00536] 0.22mm PVDF filter (Millex GV, SLGVX13NL) [00537] 100uM PEG Thiol [00538] PBS buffer (without calcium or magnesium) [00539] 20mM Sodium Acetate, pH4.3 [00540] 384-well UV Transparent Plate (Fisher Scientific, 12565506) [00541] PROCEDURE [00542] Buffer exchange and concentrate both Goat Non-specific IgG and Goat anti- human IgG into 20mM Sodium Acetate, pH4.3 by diluting antibodies into buffer and aliquoting into Amicon 30kDa MWCO centrifugal filters. Centrifuge protein solutions at 2000xg during concentration process. Atty. Dkt: RDWD-048WO [00543] Check protein concentration (e = 1.3 for Goat non-specific IgG and e = 1.9 fir Goat anti-human IgG) on nanodrop. [00544] Adjust both proteins to 0.4mg/mL with 20mM Sodium Acetate pH4.3 [00545] Mix 1 part non-specific IgG to 4 part anti-human IgG [00546] For example, mix 100 µL 0.4mg/mL Goat non-specific IgG to 400uL 0.4mg/mL Goat anti-human IgG. [00547] Mix 1 part Goat IgG mixture to 9 part 20nm Gold Nanoparticles and incubate at room temperature for 1 hour. [00548] For example, mix 500uL of the Goat antibody mixture to 4.5mL gold nanoparticles. [00549] After 1 hour incubation, add 1 part 100uM PEG Thiol to 1000 part nanoparticle solution. For example, add 5 µL to 5 mL of nanoparticle solution. [00550] Sterile filter the coated gold nanoparticle solution through the PVDF filter. The solution coming through the filter should be clear, while the gold nanoparticles should be retained in the filter. [00551] Elute the coated gold nanoparticles from the filter with 10% volume of PBS. For example, if the initial volume of coated nanoparticle solution before filtering is 5mL, elute with 0.5mL PBS. [00552] Make 2x 100 µL of test antibodies at 0.05 mg/mL by diluting protein solutions with PBS. For each 100 µL sample, add 10 µL of concentrated gold nanoparticles to each sample, mix well, and incubate at room temperature for 2 hours. [00553] For reference, add 10 µL of concentrated gold nanoparticles to 100uL of PBS and incubate for 2 hrs. After 2 hours of incubation, transfer samples and reference to individual wells in a 386-well UV transparent plate. [00554] Collect the absorbance data for each well from 450 nm to 650 nm at 2 nm increments on a plate reader. [00555] Calculate the score (lmax- lPBS) for each well. [00556] l_max = wavelength with the maximum absorption for the well [00557] l_PBS = wavelength with the maximum absorption for PBS Atty. Dkt: RDWD-048WO [00558] Self-interaction nanoparticle spectroscopy (AC-SINS) assay tests the propensity of antibodies to self-associate, which has been identified as an unfavorable property for therapeutic drug candidates. Thus, AC-SINS assay is conducted to test colloidal stability of antibodies. FIGS.5 and 6 provide the results of AC-SINS assay for triple-tagged anti-HER2 and anti-NaPi2b antibodies. These data show that adding three aldehyde tags in the specified locations and combinations did not increase the antibodies’ propensity to self-associate. Thus, from this analysis, the triple tag antibodies show favorable biophysical characteristics. Example 6 – Stability of certain antibodies disclosed herein [00559] Differentially scanning fluorimetry was used to test stability of antibodies described herein. Antibody (10 µL at 1 mg/mL) was used for protein melting temperature measurement using the Protein Thermal Shift Kit (Applied Biosystems). The antibody was mixed with 5 µL of buffer and 2.5 µL of 8X fluorescent dye for a 20 µL reaction. A QuantStudio3 (Applied Biosystems) real-time PCR machine was used to generate a melting curve. The setting was: 25°C hold for 2 min, followed by 0.05 °C/sec temperature increase to 99°C, followed by a 2 min hold at 99°C. The raw data were analyzed by Protein Thermal Shift software (Applied Biosystems). [00560] Melting temperature of an antibody can be used to test its biophysical stability. Higher melting temperatures may indicate improved biophysical characteristics. FIGS.7-9 provide melting temperature analyses for certain triple-tagged anti-HER2 and anti-NaPi2b antibodies and comparators described herein. These data show that the average melting temperatures (Tm1 and Tm2) of the triple-tagged anti-HER2 and anti-NaPi2b antibodies are similar (within 10%) of the melting temperatures observed with their wild-type (untagged) counterparts. Example 7 – Improved specificity of certain triple-tagged antibodies disclosed herein [00561] This protocol describes the Polyreactivity ELISA protocol of antibodies against DNA and Insulin [00562] REFERENCES/MATERIALS REQUIRED [00563] Insulin (Sigma-Aldrich, Cat# I9278-5mL) Atty. Dkt: RDWD-048WO [00564] Double Stranded DNA (Fisher Scientific, Cat# 26-201-21GM) [00565] Nunc Maxisorp 96-well ELISA plates (ThermoFisher, Cat# 439454) [00566] HRP-conjugated Goat Anti-Human IgG (Sigma-Aldrich, Cat# A0170) [00567] TMB ELISA Substrate Solution (ThermoFisher, Cat# 34029) [00568] 0.16M Sulfuric Acid [00569] PBS, pH7.4 + 0.05% Tween-20 + 1mM EDTA (ELISA Buffer) [00570] PBS [00571] MilliQ water [00572] PROCEDURE [00573] Diluted stock solutions of double stranded DNA to 10 µg/mL and insulin to 5 µg/mL. Made enough of both solutions to cover appropriate number of wells with 100 µL of solution. [00574] On the Nunc Maxisorp 96-well ELISA plates, added 100 µL of DNA solution into each well. On another plate, added 100 µL of insulin solution into each well. [00575] Incubated the plates overnight at room temperature with agitation. Next day, washed wells in each plate with MilliQ water three times. Added 200 µL of ELISA buffer into each well and incubated at room temperature for 1 hr with agitation. [00576] Washed wells in each plate with MilliQ water three times. Diluted test antibodies to 1 µg/mL and made a series of serial dilutions to test appropriate concentrations. A two-fold serial dilution was made. [00577] Added 100 µL of diluted antibodies into the wash plates with antigens and incubate at room temperature for 2 hrs, with agitation. Washed wells in each plate with MilliQ water three times. [00578] Add 100 µL of HRP-conjugated goat anti-human antibody that has been diluted in ELISA Buffer (1:20,000 dilution) into each well and incubated at room temperature for 1 hr with agitation. [00579] Washed wells in each plate with MilliQ water three times. Added 100 µL of TMB solution into each well and incubate for 5 minutes. After 5 minutes, add 50 µL of 0.16 M sulfuric acid into each well to quench the reaction. Measured the OD at 450 nm for each well. Atty. Dkt: RDWD-048WO Polyreactivity is an undesirable characteristic of antibodies and indicates non-specific binding tendencies of the antibodies, which has been identified as an unfavorable property for therapeutic drugs. FIGS.10 to 13 provide polyreactivity of certain triple-tagged antibodies disclosed herein for insulin or DNA. These data show that introducing three aldehyde tags into an antibody does not significantly increase association of that antibody with insulin, but that some configurations of triple-tagged antibodies may have increased interactions with DNA as compared to untagged, wild-type antibodies. [00580] Example 8 – Rat Pharmacokinetic Studies [00581] Study design: Sprague-Dawley rats (3/group) were given a single i.v. bolus dose of 3 mg/kg of ADCs comprising tagged trastuzumab conjugated to Compound 43. Plasma samples were collected at the designated times and were analyzed for total antibody and total ADC concentrations. [00582] Pharmacokinetic sample analysis: The concentrations of total antibody and total ADC (DAR-sensitive), were quantified by ELISA as shown in the schematic (FIG.14). For total antibody, conjugates were captured with an anti-human IgG-specific antibody and detected with an HRP-conjugated anti-human Fc-specific antibody. For total ADC, conjugates were captured with an anti-human Fab-specific antibody and detected with a mouse anti-belotecan primary antibody, followed by an HRP-conjugated anti-mouse IgG-subclass 1-specific secondary antibody. Bound secondary antibody was detected using Ultra TMB One-Step ELISA substrate (Thermo Fisher). After quenching the reaction with sulfuric acid, signals were read by taking the absorbance at 450 nm on a BioTek Synergy Neo2 plate reader. [00583] Results for ADC of Compound 43 are shown in FIG.15, which shows a graph of rat pharmacokinetic data showing total antibody and total ADC concentrations as measured by ELISA in plasma samples from rats dosed with the indicated compounds and sampled at the times shown.^^ Calculated PK parameters for ADC of Compound 43 are shown in Table ^9. [00584] Table 9. Rat PK Parameters for cRW8094: HER2 CH1/CT/22A Compound 43 (Belotecan+iRGD). PK Sample AUCCO-t Kel T1/2 Dose CL Vd ) Atty. Dkt: RDWD-048WO cRW8094 HER2 CH1/CT/22A Compound 43 B l t iR D t t l A 124 E 1 4 12 1 Kel: Elimination rate constant CL: Clearance Vd: Volume distribution [00585] While the present disclosure has been described with reference to the specific embodiments thereof, it should be understood by those skilled in the art that various changes may be made and equivalents may be substituted without departing from the true spirit and scope of the present disclosure. In addition, many modifications may be made to adapt a particular situation, material, composition of matter, process, process step or steps, to the objective, spirit and scope of the present disclosure. All such modifications are intended to be within the scope of the claims appended hereto.

Claims

Atty. Dkt: RDWD-048WO CLAIMS We Claim: 1. An antibody comprising an immunoglobulin (Ig) heavy chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence, wherein the first amino acid sequence and the second amino acid sequence are selected from: SEQ ID NOs: 1 to 15, wherein, in the subsequence X¹Z¹X²Z²X³Z³ of the SEQ ID NOs: 1 to 15: X¹ is present or absent, and when present, can be any amino acid; Z¹ is cysteine, serine, 2-formylglycine (fGly), or fGly’, wherein fGly’ is an fGly residue covalently bound to a payload; Z² is proline or alanine; Z³ is an aliphatic amino acid or a basic amino acid; X² and X³ are each independently any amino acid. 2. The antibody of claim 1, wherein the first amino acid sequence and the second amino acid second sequence, respectively, comprise: SEQ ID NO: 6 and SEQ ID NO: 11; SEQ ID NO:15 and SEQ ID NO: 11; SEQ ID NO: 15 and SEQ ID NO: 1; SEQ ID NO: 9 and SEQ ID NO: 11; SEQ ID NO: 15 and SEQ ID NO: 9; SEQ ID NO: 15 and SEQ ID NO: 6; SEQ ID NO: 8 and SEQ ID NO: 11; SEQ ID NO: 8 and SEQ ID NO: 15; SEQ ID NO: 3 and SEQ ID NO: 11; SEQ ID NO: 3 and SEQ ID NO: 6; SEQ ID NO: 15 and SEQ ID NO: 5; SEQ ID NO: 5 and SEQ ID NO: 11; SEQ ID NO: 5 and SEQ ID NO: 9; or Atty. Dkt: RDWD-048WO SEQ ID NO: 12 and SEQ ID NO: 11. 3. An antibody comprising an immunoglobulin (Ig) heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and the Ig light chain comprises a second amino acid sequence, wherein the first amino acid sequence is selected from SEQ ID NOs: 1 to 15 and the second amino acid sequence is selected from SEQ ID NOs: 16 to 20, wherein, in the subsequence X¹Z¹X²Z²X³Z³ of the SEQ ID NOs: 1 to 20: X¹ is present or absent, and when present, can be any amino acid; Z¹ is cysteine, serine, 2-formylglycine (fGly), or fGly’, wherein fGly’ is an fGly residue covalently bound to a payload; Z² is proline or alanine; Z³ is an aliphatic amino acid or a basic amino acid; X² and X³ are each independently any amino acid. 4. The antibody of claim 3, wherein the first amino acid sequence and the second amino acid sequence, respectively, comprise: SEQ ID NO: 7 and SEQ ID NO: 18; SEQ ID NO: 12 and SEQ ID NO: 18; SEQ ID NO: 8 and SEQ ID NO: 18; SEQ ID NO: 11 and SEQ ID NO: 18; SEQ ID NO: 15 and SEQ ID NO: 19; SEQ ID NO: 10 and SEQ ID NO: 18; SEQ ID NO: 1 and SEQ ID NO: 18; SEQ ID NO: 5 and SEQ ID NO: 18; SEQ ID NO: 4 and SEQ ID NO: 18; SEQ ID NO: 1 and SEQ ID NO: 19; SEQ ID NO: 11 and SEQ ID NO: 19; SEQ ID NO: 5 and SEQ ID NO: 19; SEQ ID NO: 9 and SEQ ID NO: 18; Atty. Dkt: RDWD-048WO SEQ ID NO: 8 and SEQ ID NO: 19; SEQ ID NO: 15 and SEQ ID NO: 18; SEQ ID NO: 6 and SEQ ID NO: 18; SEQ ID NO: 6 and SEQ ID NO: 19; SEQ ID NO: 2 and SEQ ID NO: 18; SEQ ID NO: 12 and SEQ ID NO: 19; SEQ ID NO: 4 and SEQ ID NO: 19; SEQ ID NO: 7 and SEQ ID NO: 19; SEQ ID NO: 10 and SEQ ID NO: 19; SEQ ID NO: 4 and SEQ ID NO: 20; SEQ ID NO: 5 and SEQ ID NO: 20; SEQ ID NO: 8 and SEQ ID NO: 20; SEQ ID NO: 10 and SEQ ID NO: 20; SEQ ID NO: 2 and SEQ ID NO: 20; SEQ ID NO: 7 and SEQ ID NO: 20; SEQ ID NO: 12 and SEQ ID NO: 20; SEQ ID NO: 1 and SEQ ID NO: 20; or SEQ ID NO: 15 and SEQ ID NO: 20. 5. An antibody comprising an immunoglobulin (Ig) heavy chain and an Ig light chain, wherein the Ig heavy chain comprises a first amino acid sequence and a second amino acid sequence and the Ig light chain comprises a third amino acid sequence, wherein the first amino acid sequence and the second amino acid sequence are selected from SEQ ID NOs: 1 to 15 and the third amino acid sequence is selected from SEQ ID NOs: 16 to 20, wherein, in the subsequence X¹Z¹X²Z²X³Z³ of the SEQ ID NOs: 1 to 20: X¹ is present or absent, and when present, can be any amino acid; Z¹ is cysteine, serine, 2-formylglycine (fGly), or fGly’, wherein fGly’ is an fGly residue covalently bound to a payload; Z² is proline or alanine; Z³ is an aliphatic amino acid or a basic amino acid; Atty. Dkt: RDWD-048WO X² and X³ are each independently any amino acid. 6. The antibody of claim 5, wherein the first amino acid sequence, the second amino acid sequence, and the third amino acid sequence, respectively, comprise: SEQ ID NO: 9, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 18; SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 18; SEQ ID NO: 8, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 3, SEQ ID NO: 11, and SEQ ID NO: 18; SEQ ID NO: 3, SEQ ID NO: 6, and SEQ ID NO: 18; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 16; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 17; SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 16; SEQ ID NO: 15, SEQ ID NO: 6, and SEQ ID NO: 17; SEQ ID NO: 15, SEQ ID NO: 1, and SEQ ID NO: 19; SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 18; or SEQ ID NO: 6, SEQ ID NO: 11, and SEQ ID NO: 19. 7. The antibody of any one of claims 1 to 6, wherein Z³ is arginine. 8. The antibody of any one of claims 1 to 7, wherein X¹ is present. 9. The antibody of claim 8, wherein X¹ is glycine, leucine, isoleucine, methionine, histidine, tyrosine, valine, serine, cysteine, or threonine. 10. The antibody of any one of claims 1 to 9, wherein X² and X³ are each independently serine, threonine, alanine, valine, glycine, or cysteine. Atty. Dkt: RDWD-048WO 11. The antibody of any one of claims 1 to 10, wherein the Ig heavy chain is IgG and/or the Ig light chain is kappa light chain. 12. The antibody of any one of claims 1 to 11, wherein the antibody specifically binds a target antigen on a target cell. 13. The antibody of claim 12, wherein the target antigen on the target cell is a tumor antigen on a cancer cell. 14. The antibody of claim 12, wherein the target antigen on the target cell is an immunogen on an immune cell. 15. The antibody of any one of claims 1 to 14, wherein the subsequence X¹Z¹X²Z²X³Z³ of the SEQ ID NOs: 1 to 20 is LCTPSR (SEQ ID NO: 22) or LSTPSR (SEQ ID NO: 23). 16. The antibody of any one of claims 1 to 14, wherein the subsequence X¹Z¹X²Z²X³Z³ of the SEQ ID NOs: 1 to 20 is L(fGly)TPSR (SEQ ID NO: 90). 17. The antibody of any one of claims 1 to 14, wherein the subsequence X¹Z¹X²Z²X³Z³ of the SEQ ID NOs: 1 to 20 is selected from MCTPSR (SEQ ID NO: 24), VCTPSR (SEQ ID NO: 25), LCSPSR (SEQ ID NO: 26), LCAPSR (SEQ ID NO: 27), LCVPSR (SEQ ID NO: 28), LCGPSR (SEQ ID NO: 29), ICTPAR (SEQ ID NO: 30), LCTPSK (SEQ ID NO: 31), MCTPSK (SEQ ID NO: 32), VCTPSK (SEQ ID NO: 33), LCSPSK (SEQ ID NO: 34), LCAPSK (SEQ ID NO: 35), LCVPSK (SEQ ID NO: 36), LCGPSK (SEQ ID NO: 37), LCTPSA (SEQ ID NO: 38), ICTPAA (SEQ ID NO: 39), MCTPSA (SEQ ID NO: 40), VCTPSA (SEQ ID NO: 41), LCSPSA (SEQ ID NO: 42), LCAPSA (SEQ ID NO: 43), LCVPSA (SEQ ID NO: 44), LCGPSA (SEQ ID NO: 45), MSTPSR (SEQ ID NO: 46), VSTPSR (SEQ ID NO: 47), LSSPSR (SEQ ID NO: 48), LSAPSR (SEQ ID NO: 49), LSVPSR (SEQ ID NO: 50), LSGPSR (SEQ ID NO: 51), ISTPAR (SEQ ID NO: 52), LSTPSK (SEQ ID NO: 53), MSTPSK (SEQ ID NO: 54), VSTPSK (SEQ ID NO: 55), LSSPSK (SEQ ID NO: 56), LSAPSK (SEQ ID NO: 57), LSVPSK (SEQ ID NO: 58), LSGPSK (SEQ ID NO: 59), LSTPSA (SEQ ID NO: 60), ISTPAA (SEQ ID NO: 61), MSTPSA (SEQ ID NO: 62), VSTPSA (SEQ ID NO: Atty. Dkt: RDWD-048WO 63), LSSPSA (SEQ ID NO: 64), LSAPSA (SEQ ID NO: 65), LSVPSA (SEQ ID NO: 66), and LSGPSA (SEQ ID NO: 67). 18. The antibody of claim 17, wherein the subsequence X¹Z¹X²Z²X³Z³ is selected from M(fGly)TPSR (SEQ ID NO: 68), V(fGly)TPSR (SEQ ID NO: 69), L(fGly)SPSR (SEQ ID NO: 70), L(fGly)APSR (SEQ ID NO: 71), L(fGly)VPSR (SEQ ID NO: 72), L(fGly)GPSR (SEQ ID NO: 73), I(fGly)TPAR (SEQ ID NO: 74), L(fGly)TPSK (SEQ ID NO: 75), M(fGly)TPSK (SEQ ID NO: 76), V(fGly)TPSK (SEQ ID NO: 77), L(fGly)SPSK (SEQ ID NO: 78), L(fGly)APSK (SEQ ID NO: 79), L(fGly)VPSK (SEQ ID NO: 80), L(fGly)GPSK (SEQ ID NO: 81), L(fGly)TPSA (SEQ ID NO: 82), I(fGly)TPAA (SEQ ID NO: 83), M(fGly)TPSA (SEQ ID NO: 84), V(fGly)TPSA (SEQ ID NO: 85), L(fGly)SPSA (SEQ ID NO: 86), L(fGly)APSA (SEQ ID NO: 87), L(fGly)VPSA (SEQ ID NO: 88), L(fGly)GPSA (SEQ ID NO: 89), and L(fGly)TPSR (SEQ ID NO: 90). 19. The antibody of any one of claims 1 to 14, wherein Z¹ is fGly’ and wherein the antibody is covalently conjugated to a first payload via fGly’. 20. The antibody of claim 19, wherein the conjugation of the fGly to the first payload provides an average molar ratio of the first payload to the antibody of at least 0.5 per fGly present in the antibody. 21. The antibody of claim 20, wherein the antibody is covalently conjugated to the first payload via a hydrazone, oxime, semicarbazone, alkyl, alkenyl, acyloxy, hydrazinyl-indolyl, hydrazinyl-imidazoyl, hydrazinyl-pyrrolyl, hydrazinyl-furanyl, or a pyrazalinone linkage. 22. The antibody of claim 20, wherein the antibody is covalently conjugated to the first payload via a linking group. 23. The antibody of claim 22, wherein the linking group is a branched hydrazino-iso-pictet- spengler (HIPS) or a tandem-cleavage linker. Atty. Dkt: RDWD-048WO 24. The antibody of claim 19, further comprising a second payload conjugated to an intrachain cysteine residue. 25. The antibody of claim 24, wherein the second payload is conjugated to the intrachain cysteine residue via a different linker than the covalent conjugation between the first payload and the fGly’. 26. The antibody of any one of claims 19 to 23, wherein the first payload is selected from a small molecule drug, a detectable label, a water-soluble polymer, a synthetic peptide, a protein degrader, an oligonucleotide, a radiolabeled ligand, and an antimicrobial. 27. The antibody of any one of claims 19 to 25, wherein the first payload is a small molecule drug. 28. The antibody of claim 27, wherein the small molecule drug is an immunomodulator, a cytotoxic molecule, or a cancer chemotherapeutic agent. 29. The antibody of claim 28, wherein the small molecule drug is the cancer therapeutic agent. 30. The antibody of claim 29, wherein the cancer chemotherapeutic agent is an alkylating agent, a microtubule inhibitor, topoisomerase inhibitor, kinase inhibitor, a nitrosourea, an antimetabolite, an antitumor antibiotic, a vinca alkaloid, or a steroid hormone. 31. The antibody of claim 26, wherein the first payload is the water-soluble polymer. 32. The antibody of claim 31, wherein the water-soluble polymer is poly(ethylene glycol). 33. The antibody of claim 26, wherein the first payload is the detectable label. Atty. Dkt: RDWD-048WO 34. The antibody of claim 33, wherein the detectable label is an imaging agent. 35. The antibody of claim 34, wherein the imaging agent is a radiolabeled ligand. 36. The antibody of claim 26, wherein the first payload is the antimicrobial agent. 37. The antibody of claim 36, wherein the antimicrobial agent is an antiviral, an antibacterial, or an antifungal. 38. The antibody of claim 37, wherein the antiviral is a viral fusion inhibitor. 39. The antibody of any one of claims 1 to 38, wherein the antibody is derived from an antibody selected from Trastuzumab, Polatuzumab, Gemtuzumab, anti-NaPi2b antibody, and anti-SGN-33a antibody. 40. A recombinant nucleic acid comprising a nucleotide sequence encoding an antibody of any one of claims 1 to 14, wherein Z¹ is cysteine or serine. 41. The recombinant nucleic acid of claim 40, wherein the nucleotide sequence encodes the heavy chain comprising a heavy chain variable region and the heavy chain constant region of the antibody and, when present, the light chain comprising a light chain variable region and a light chain constant region. 42. A recombinant expression vector comprising the recombinant nucleic acid of claim 40 or 41, wherein the antibody-encoding nucleotide sequence is operably linked to a promoter. 43. A host cell genetically modified to express an antibody of any one of claims 1 to 18. 44. The host cell of claim 43, genetically modified to express a formylglycine generating enzyme (FGE), in a manner sufficient to convert the antibody into an fGly-modified antibody. Atty. Dkt: RDWD-048WO 45. The host cell of claim 43 or 44, wherein the host cell is a mammalian cell, yeast cell, insect cell, or a bacterial cell. 46. The host cell of claim 45, wherein the bacterial cell is Escherichia coli. 47. A method of producing an antibody conjugate, comprising: combining, in a reaction mixture: the antibody of any one of claims 1 to 18, wherein Z¹ is fGly’; and a reactive partner comprising a payload and an aldehyde-reactive group, said combining under conditions sufficient for the aldehyde-reactive group to react with an aldehyde group of the fGly residue thereby conjugating the payload to the fGly residue via a covalent linkage to generate the antibody conjugate; and isolating the antibody conjugate from the reaction mixture. 48. The method of claim 47, wherein the aldehyde-reactive group is selected from the group consisting of: a hydrazine, hydrazide, aminooxy, semicarbazide, hydrazinyl-indole, hydrazinyl-imidazole, hydrazinyl-pyrrole, hydrazinyl-furan, and a pyrazalinone group. 49. The method of claim 47 or 48, wherein the reactive partner comprises a linking group covalently linking the aldehyde-reactive group with the payload. 50. The method of claim 49, wherein the linking group is a branched hydrazino-iso-pictet- spengler (HIPS) or a tandem-cleavage linker. 51. An antibody conjugate produced by the method of any one of claims 47 to 50. 52. A formulation comprising: the antibody of any one of claims 1 to 39, or the antibody conjugate of claim 51; and a pharmaceutically acceptable excipient. Atty. Dkt: RDWD-048WO 53. A method of treating a disease in a subject, comprising administering to the subject a therapeutically effective amount of the antibody of any one of claims 1 to 14, the antibody conjugate of claim 51, or the formulation of claim 52. 54. The method of claim 53, wherein the disease is a cancer, an autoimmune disease, an infection. 55. A method of preventing a disease in a subject, comprising administering to the subject a therapeutically effective amount of the antibody of any one of claims 1 to 14, the antibody conjugate of claim 51, or the formulation of claim 52. 56. The method of claim 55, wherein the disease is a cancer or an infection.