Antibody compositions and uses thereof

Abstract

Aspects of the disclosure provide a composition comprising a stress-sensitive antibody formulated with histidine and optionally methionine in amounts effective to promote resistance of the antibody to light stress and / or thermal stress.

Description

ANTIBODY COMPOSITIONS AND USES THEREOFRELATED APPLICATIONS

[0001] This application claims the benefit under 35 U.S.C. § 119(e) of U.S. Provisional Application No. 63 / 725,739 filed November 27, 2024, entitled “ANTIBODY FORMULATION AND USES THEREOF”, the content of which is hereby incorporated by reference in its entirety.REFERENCE TO AN ELECTRONIC SEQUENCE LISTING

[0002] The content of the electronic sequence listing (D084270014WO00-SEQ-KGC.xml; Size: 86,811; and Date of Creation: November 25, 2025) is incorporated by reference herein in its entirety.BACKGROUND

[0003] There is a need for improved antibody-containing compositions that promote resistance to stress conditions. Compositions that comprise antibodies may undergo environmental stresses during storage, transportation, and handling. These environmental stresses can include heat, agitation, and / or light stress. It is important to maintain the purity and integrity of antibodies within the composition.SUMMARY

[0004] Certain aspects of the disclosure relate to a recognition that antibodies sensitive to environmental stresses (e.g., thermal, agitation, and / or light stress) may be stabilized in certain formulations (e.g., formulations comprising particular concentrations of certain components, such as amino acids). In some embodiments, compositions provided herein are useful for promoting resistance of stress-sensitive antibodies to environmental stresses. In some embodiments, a stressor is thermal stress (e.g., heat), agitation, and / or light stress (e.g., visible light or UV light).

[0005] In some aspects, provided herein are compositions comprising a stress-sensitive antibody formulated with histidine in amounts effective to promote resistance of the antibody to light stress and / or thermal stress. In some embodiments, the composition further comprises methionine. In some embodiments, the molar ratio of histidine to the antibody in the composition is in the range of 12: 1-160: 1. In some embodiments, the molar ratio of methionine to the antibody in the composition is in the range of 0: 1-20: 1.

[0006] In some embodiments, the composition is a solution.1#14616800v2

[0007] In some embodiments, the composition comprises the antibody at a concentration in the range of 120-500 mg / mL. In some embodiments, the composition comprises the antibody at a concentration of 175 mg / mL. In some embodiments, the composition comprises the antibody at a concentration of 150 mg / mL.

[0008] In some embodiments, the composition comprises histidine at a concentration in the range of 45-150 mM. In some embodiments, the composition comprises histidine at a concentration in the range of 50-100 mM. In some embodiments, the composition comprises histidine at a concentration of 50 mM. In some embodiments, the composition comprises histidine at a concentration of 100 mM. In some embodiments, the histidine is L-histidine, D- histidine, or any salt hereof. In some embodiments, the histidine is histidine hydrocholoride, histidine sulfate, or histidine acetate.

[0009] In some embodiments, the composition comprises methionine at a concentration in the range of 0-20 mM. In some embodiments, the composition comprises methionine at a concentration of 10 mM. In some embodiments, the methionine is L-methionine, D- methionine, or any salt thereof.

[0010] In some embodiments, the composition further comprises arginine. In some embodiments, the composition comprises arginine at a concentration in the range of 10-500 mM. In some embodiments, the composition comprises arginine at a concentration in the range of 50-200 mM. In some embodiments, the composition comprises arginine at a concentration of 150 mM.

[0011] In some embodiments, the composition further comprises a sugar. In some embodiments, the sugar is sucrose, maltose, or trehalose. In some embodiments, the sugar is sucrose. In some embodiments, the composition comprises sucrose in the range of 1% to 5% (w / v).

[0012] In some embodiments, the composition further comprises a surfactant. In some embodiments, the surfactant is sodium dodecyl sulfate (SDS), polysorbate, or nonionic surfactant. In some embodiments, the surfactant is polysorbate 20 or polysorbate 80. In some embodiments, the composition comprises polysorbate in the range of 0.005% to 0.05% (w / v).

[0013] In some embodiments, the composition has a pH in the range of 5-7. In some embodiments, the composition has a pH of 5.6.

[0014] In some embodiments, the composition is lyophilized.

[0015] In some embodiments, the antibody is stable in the composition at 40 °C for at least two weeks.2#14616800v2

[0016] In some embodiments, the antibody is stable when the composition is exposed to light at an intensity of at least 3000 lux for at least 10 days. In some embodiments, the antibody is stable when the composition is exposed to UV light for at least 50 hours.

[0017] In some embodiments, the antibody is stable after being agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days. In some embodiments, the antibody is stable after the composition is stored at 40°C for at least 10 days after agitation.

[0018] In some embodiments, the antibody in the composition retains purity of at least 93% after being subjected to 40 °C for at least two weeks, exposed to light at an intensity of at least 3000 lux for at least 10 days, exposed to UV light for at least 50 hours, agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days, or any combination thereof.

[0019] In some embodiments, the composition comprises less than 7% high molecular weight aggregates after being subjected to 40 °C for at least two weeks, exposed to light at an intensity of at least 3000 lux for at least 10 days, exposed to UV light for at least 50 hours, agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days, or any combination thereof.

[0020] In some embodiments, the composition comprises less than 0.7% low molecular weight impurities after being subjected to 40 °C for at least two weeks, exposed to light at an intensity of at least 3000 lux for at least 10 days, exposed to UV light for at least 50 hours, agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days, or any combination thereof.

[0021] In some embodiments, the composition comprises less than 7000 counts / mL sub- visible particles that are at least 2 pm in size after being subjected to 40 °C for at least two weeks, exposed to light at an intensity of at least 3000 lux for at least 10 days, exposed to UV light for at least 50 hours, agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days, or any combination thereof. In some embodiments, the composition comprises less than 500 counts / mL sub-visible particles that are at least 5 pm in size after being subjected to 40 °C for at least two weeks, exposed to light at an intensity of at least 3000 lux for at least 10 days, exposed to UV light for at least 50 hours, agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days, or any combination thereof.

[0022] In some embodiments, the composition has a viscosity of less than 15 mPa-s after being subjected to 40 °C for at least two weeks, exposed to light at an intensity of at least 3000 lux for at least 10 days, exposed to UV light for at least 50 hours, agitated at a speed in the range of 100-1000 rpm at 40 °C for at least 3 days, or any combination thereof.3#14616800v2

[0023] In some embodiments, the antibody comprises methionine or tryptophan in a complementarity determining region (CDR).

[0024] In some embodiments, the antibody comprises at least one amino acid residue capable of undergoing a post-translational modification (PTM). In some embodiments, the PTM is pyro-glutamic acid, oxidation, di-oxidation, oxidation-C6H5N, isomerization, dioxi dation-HCN, glycation, deamidation, or succinimide formation. In some embodiments, the composition reduces and / or prevents the PTM.

[0025] In some embodiments, the antibody is an anti-TMPRSS6 antibody. In some embodiments, the antibody comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 24, a HC CDR2 having the amino acid sequence of SEQ ID NO: 48, a HC CDR3 having the amino acid sequence of SEQ ID NO: 26, a LC CDR1 having the amino acid sequence of SEQ ID NO: 27, a LC CDR2 having the amino acid sequence of WAT, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 29. In some embodiments, the antibody comprises a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 49, and a light chain variable domain having the amino acid sequence of SEQ ID NO: 50. In some embodiments, the antibody comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 52, and a light chain comprising the amino acid sequence of SEQ ID NO: 53.

[0026] Provided herein, in some aspects, is a prefilled syringe comprising a composition disclosed herein. In some embodiments, the prefilled syringe is a glass syringe.

[0027] The foregoing and other aspects, implementations, acts, functionalities, features and embodiments of the present teachings can be more fully understood from the following description.DETAILED DESCRIPTION

[0028] The present disclosure, at least in part, relates to a recognition that compositions (e.g., compositions comprising an antibody) formulated with effective amounts of certain amino acids (e.g., histidine and / or methionine) can promote resistance of an antibody (e.g., stress-sensitive antibody) to certain environmental stress (e.g., thermal, agitation, and / or light stress). In some embodiments, the present disclosure relates to a composition comprising: a stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody described herein) at a high concentration (e.g., more than 100 mg / mL), histidine, and optionally methionine in amounts effective to promote resistance of the antibody to stress conditions (e.g., light and / or thermal stress).4#14616800v2

[0029] In some embodiments, compositions provided herein are useful for stabilizing antibodies (e.g., stress-sensitive antibodies) when subjected to stressors. In some embodiments, a stressor comprises thermal stress (e.g., temperature of 40°C or higher), agitation, and / or light stress (e.g., bright visible light or UV light). In some embodiments, compositions provided herein comprise histidine. In some embodiments, compositions provided herein comprise histidine and methionine. In some embodiment, compositions provided herein comprise histidine and do not comprise methionine. In some embodiments, compositions provided herein further comprise a surfactant and / or a sugar.

[0030] In some embodiments, compositions provided herein stabilize a stress-sensitive antibody described herein by one or more of the following: decreasing post-translational modifications of the antibody, decreasing the formation of low molecular weight degradation species of the antibody, and / or decreasing the formation of high molecular weight aggregates of the antibody.

[0031] In some embodiments, a composition comprising a stress-sensitive antibody described herein has lower viscosity relative to a different composition comprising the same antibody in a different formulation. In some embodiments, the appearance of a composition comprising a stress-sensitive antibody described herein has an improved appearance (e.g., less yellowing in color) relative to a different composition comprising the same antibody in a different formulation. In some embodiments, a composition comprising a stress-sensitive antibody described herein is less turbid (e.g., contains fewer sub-visible particles) relative to a different composition comprising the same antibody in a different formulation.

[0032] In some embodiments, an antibody is an anti-TMPRSS6 antibody (e.g., an anti- TMPRSS6 antibody comprising a heavy chain comprising the amino acid sequence of SEQ ID NO: 52, and a light chain comprising the amino acid sequence of SEQ ID NO: 53).

[0033] Further aspects of the disclosure, including a description of defined terms, are provided below.I. Definitions

[0034] And / or: As used herein, the term “and / or” is to be taken as specific disclosure of each of the two or more specified features or components with or without the other. Thus, the term “and / or” as used in a phrase such as “A and / or B” herein is intended to include “A and B,” “A or B,” “A” (alone), and “B” (alone). Likewise, the term “and / or” as used in a phrase such as “A, B, and / or C” is intended to encompass each of the following aspects: A, B, and5#14616800v2C; A, B, or C; A or C; A or B; B or C; A and C; A and B; B and C; A (alone); B (alone); and C (alone).

[0035] Administering: As used herein, the terms, “administer”, “administered”, “administering” or “administration” means to provide an antibody or a composition thereof to a subject in a manner that is physiologically and / or pharmacologically useful (e.g., to treat a condition in the subject).

[0036] Affinity Matured Antibody: The term “Affinity Matured Antibody” is used herein to refer to an antibody with one or more alterations in one or more CDRs, which result in an improvement in the affinity (e.g., KD, kd or ka) of the antibody for a target antigen compared to a parent antibody, which does not possess the alteration(s). Exemplary affinity matured antibodies may have nanomolar or even picomolar affinities for the target antigen in some embodiments. A variety of procedures for producing affinity matured antibodies are known in the art, including the screening of a combinatory antibody library that has been prepared using bio-display. For example, Marks et al., BioTechnology, 10: 779-783 (1992) describes affinity maturation by VH and VL domain shuffling. Random mutagenesis of CDR and / or framework residues is described by Barbas et al., Proc. Nat. Acad. Sci. USA, 91 : 3809-3813 (1994); Schier et al., Gene, 169: 147-155 (1995); Yelton et al., J. Immunol., 155: 1994-2004 (1995); Jackson et al., J. Immunol., 154(7): 3310-3319 (1995); and Hawkins et al, J. Mol. Biol., 226: 889-896 (1992). Selective mutation at selective mutagenesis positions and at contact or hypermutation positions with an activity-enhancing amino acid residue is described in U.S. Pat. No. 6,914,128 Bl.

[0037] Antibody: As used herein, the term “antibody” refers to a polypeptide that comprises at least one immunoglobulin variable domain which comprises at least one distinct antigen-binding site, e.g., paratope, that specifically binds to an antigen. In some embodiments, an antibody comprises a paratope. In some embodiments, a paratope comprise one or more complementarity determining region (CDRs). In some embodiments, an antibody is a full-length antibody. In some embodiments, an antibody is a chimeric antibody. In some embodiments, an antibody is a humanized antibody. However, in some embodiments, an antibody is a Fab fragment, a F(ab')2 fragment, a Fv fragment or a scFv fragment. In some embodiments, an antibody is a nanobody derived from a camelid antibody or a nanobody derived from shark antibody. In some embodiments, an antibody is a diabody. In some embodiments, an antibody comprises a framework having a human germline sequence.6#14616800v2

[0038] In another embodiment, an antibody comprises a heavy chain constant region selected from the group consisting of IgG, IgGl, IgG2, IgG2A, IgG2B, IgG2C, IgG3, IgG4, IgAl, IgA2, IgD, IgM, and IgE constant regions. In some embodiments, an antibody comprises a heavy (H) chain variable region (abbreviated herein as VH), and / or a light (L) chain variable region (abbreviated herein as VL). In some embodiments, an antibody comprises a constant region, e.g., an Fc region. An immunoglobulin constant region refers to a heavy or light chain constant region. Human IgG heavy chain and light chain constant region amino acid sequences and their functional variations are known. With respect to the heavy chain, in some embodiments, the heavy chain of an antibody described herein can be an alpha (a), delta (A), epsilon (s), gamma (y) or mu (p) heavy chain. In some embodiments, the heavy chain of an antibody described herein can comprise a human alpha (a), delta (A), epsilon (s), gamma (y) or mu (p) heavy chain. In a particular embodiment, an antibody described herein comprises a human gamma 1 CHI, CH2, and / or CH3 domain. In some embodiments, the amino acid sequence of the heavy chain comprises the amino acid sequence of a human gamma (y) heavy chain constant region, such as any known in the art. Non-limiting examples of human constant region sequences have been described in the art, e.g., see U.S. Pat. No. 5,693,780 and Kabat E A et al., (1991) supra. In some embodiments, an antibody comprises a heavy chain that comprises an amino acid sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or at least 99% identical to any of the variable chain constant regions provided herein. In some embodiments, an antibody comprises a light chain that comprises an amino acid sequence that is at least 70%, 75%, 80%, 85%, 90%, 95%, 98%, or at least 99% identical to any of the light chain constant regions provided herein.

[0039] In some embodiments, an antibody is modified, e.g., modified via glycosylation, phosphorylation, sumoylation, and / or methylation. In some embodiments, an antibody is a glycosylated antibody, which is conjugated to one or more sugar or carbohydrate molecules. In some embodiments, the one or more sugar or carbohydrate molecule are conjugated to the antibody via N-glycosylation, O-glycosylation, C-glycosylation, glypiation (GPI anchor attachment), and / or phosphoglycosylation. In some embodiments, the one or more sugar or carbohydrate molecule are monosaccharides, disaccharides, oligosaccharides, or glycans. In some embodiments, the one or more sugar or carbohydrate molecule is a branched oligosaccharide or a branched glycan. In some embodiments, the one or more sugar or carbohydrate molecule includes a mannose unit, a glucose unit, an N-acetylglucosamine unit, or a phospholipid unit.7#14616800v2

[0040] In some embodiments, an antibody is a construct that comprises a polypeptide comprising one or more antigen binding fragments of the disclosure linked to a linker polypeptide or an immunoglobulin constant domain. Linker polypeptides comprise two or more amino acid residues joined by peptide bonds and are used to link one or more antigen binding portions. Examples of linker polypeptides have been reported (see e.g., Holliger, P, et al. (1993) Proc. Natl. Acad. Sci. USA 90:6444-6448; Poljak, R. J., et al. (1994) Structure 2: 1121-1123). Still further, an antibody may be part of a larger immunoadhesion molecule, formed by covalent or noncovalent association of the antibody or antibody portion with one or more other proteins or peptides. Examples of such immunoadhesion molecules include use of the streptavidin core region to make a tetrameric scFv molecule (Kipriyanov, S. M., et al. (1995) Human Antibodies and Hybridomas 6:93-101) and use of a cysteine residue, a marker peptide and a C-terminal polyhistidine tag to make bivalent and biotinylated scFv molecules (Kipriyanov, S. M., et al. (1994) Mol. Immunol. 31 : 1047-1058).

[0041] Approximately: As used herein, the term “approximately” or “about,” as applied to one or more values of interest, refers to a value that is similar to a stated reference value. In certain embodiments, the term “approximately” or “about” refers to a range of values that fall within 20%, 19%, 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1%, or less in either direction (greater than or less than) of the stated reference value unless otherwise stated or otherwise evident from the context (except where such number would exceed 100% of a possible value).

[0042] CDR: As used herein, the term "CDR" refers to the complementarity determining region within antibody variable sequences. Atypical antibody molecule comprises a heavy chain variable region (VH) and a light chain variable region (VL), which are usually involved in antigen binding. The VH and VL regions can be further subdivided into regions of hypervariability, also known as “complementarity determining regions” (“CDR”), interspersed with regions that are more conserved, which are known as “framework regions” (“FR”). Each VH and VL is typically composed of three CDRs and four FRs, arranged from amino-terminus to carboxy -terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. The extent of the framework region and CDRs can be precisely identified using methodology known in the art, for example, by the Kabat definition, the IMGT definition, the Chothia definition, the AbM definition, and / or the Contact definition, all of which are well known in the art, see, e.g., Kabat, E.A., et al. (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242; IMGT®, the international ImMunoGeneTics information system® www.imgt.org,8#14616800v2Lefranc, M.-P. et al., Nucleic Acids Res., 27:209-212 (1999); Ruiz, M. et al., Nucleic Acids Res., 28:219-221 (2000); Lefranc, M.-P, Nucleic Acids Res., 29:207-209 (2001); Lefranc, M - P, Nucleic Acids Res., 31:307-310 (2003); Lefranc, M.-P. et al., In Silico Biol., 5, 0006 (2004), 5:45-60 (2005); Lefranc, M.-P. et al., Nucleic Acids Res., 33:D593-597 (2005); Lefranc, M.-P. et al., Nucleic Acids Res., 37:D1006-1012 (2009); Lefranc, M.-P. et al., Nucleic Acids Res., 43:D413-422 (2015); Chothia et al., (1989) Nature 342:877; Chothia, C. et al. (1987) J. Mol. Biol. 196:901-917, Al-lazikani et al (1997) J. Molec. Biol. 273:927-948; and Almagro, J. Mol. Recognit. 17: 132-143 (2004). See also: hgmp.mrc.ac.uk and bioinf.org.uk / abs. As used herein, a CDR may refer to the CDR defined by any method known in the art. Two antibodies having the same CDR means that the two antibodies have the same amino acid sequence of that CDR as determined by the same method, for example, the IMGT definition.

[0043] In certain embodiments, there are three CDRs in each of the variable regions of a heavy chain (HC) and a light chain (LC), which are designated CDR1, CDR2 and CDR3, for each of the variable regions. The term "CDR set" as used herein refers to a group of three CDRs that occur in a single variable region capable of binding the antigen. The exact boundaries of these CDRs have been defined differently according to different systems. The system described by Kabat (Kabat et al., Sequences of Proteins of Immunological Interest (National Institutes of Health, Bethesda, Md. (1987) and (1991)) not only provides an unambiguous residue numbering system applicable to any variable region of an antibody, but also provides precise residue boundaries defining the three CDRs. These CDRs may be referred to as Kabat CDRs. Sub-portions of CDRs may be designated as LI, L2 and L3 or Hl, H2 and H3 where the "L" and the "H" designate the light chain and the heavy chains regions, respectively. These regions may be referred to as Chothia CDRs, which have boundaries that overlap with Kabat CDRs. Other boundaries defining CDRs overlapping with the Kabat CDRs have been described by Padlan (FASEB J. 9: 133-139 (1995)) and MacCallum (J Mol Biol 262(5):732-45 (1996)). Still other CDR boundary definitions may not strictly follow one of the above systems, but will nonetheless overlap with the Kabat CDRs, although they may be shortened or lengthened in light of prediction or experimental findings that particular residues or groups of residues or even entire CDRs do not significantly impact antigen binding. The methods used herein may utilize CDRs defined according to any of these systems, although preferred embodiments use Kabat or Chothia defined CDRs.9#14616800v2

[0044] In certain embodiments, the CDRs of an antibody may have different amino acid sequences when different definition systems are used (e.g., the IMGT definition, the Kabat definition, or the Chothia definition). A definition system annotates each amino acid in a given antibody sequence (e.g., VH or VL sequence) with a number, and numbers corresponding to the heavy chain and light chain CDRs are provided in Table 2. The CDRs listed in Table 1 are defined in accordance with the Kabat definition. One skilled in the art is able to derive the CDR sequences using the different numbering systems for the anti- TMPRSS6 antibodies provided in Table 1.Table 2. CDR Definitions1IMGT®, the international ImMunoGeneTics information system®, imgt.org, Lefranc, M.-P. et al., Nucleic Acids Res. , 27:209-212 (1999)2Kabat et al. (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-32423Chothia et al., J. Mol. Biol. 196:901-917 (1987)

[0045] CDR-grafted antibody: The term "CDR-grafted antibody" refers to an antibody that comprises a VH and a VL from a first species in which the sequences of one or more of the CDRs regions of the VH and / or the VL are replaced with CDR sequences of another species; for example, a CDR-grafted antibody may comprise a murine VH and VL in which one or more of the murine CDRs (e.g., CDR3) has been replaced with a human CDR sequence.

[0046] Chimeric antibody: The term "chimeric antibody" refers to antibodies which comprise a VH and VL from one species and a constant region (e.g., heavy chain constant region) from another species; for example, a chimeric antibody may comprise a murine VH and VL linked to a human constant region (e.g., a human heavy chain constant region).

[0047] Complementary: As used herein, the term “complementary” refers to the capacity for precise pairing between two nucleotides or two sets of nucleotides. In particular, complementary is a term that characterizes an extent of hydrogen bond pairing that brings about binding between two nucleotides or two sets of nucleotides. For example, if a base at10#14616800v2one position of an oligonucleotide is capable of hydrogen bonding with a base at the corresponding position of a target nucleic acid (e.g., an mRNA), then the bases are considered to be complementary to each other at that position. Base pairings may include both canonical Watson-Crick base pairing and non-Watson-Crick base pairing (e.g., Wobble base pairing and Hoogsteen base pairing). For example, in some embodiments, for complementary base pairings, adenosine-type bases (A) are complementary to thymidine- type bases (T) or uracil-type bases (U), that cytosine-type bases (C) are complementary to guanosine-type bases (G), and that universal bases such as 3 -nitropyrrole or 5-nitroindole can hybridize to and are considered complementary to any A, C, U, or T. Inosine (I) has also been considered in the art to be a universal base and is considered complementary to any A, C, U or T.

[0048] Conservative amino acid substitution: As used herein, a “conservative amino acid substitution” refers to an amino acid substitution that does not alter the relative charge or size characteristics of the protein in which the amino acid substitution is made. Variants can be prepared according to methods for altering polypeptide sequence known to one of ordinary skill in the art such as are found in references which compile such methods, e.g. Molecular Cloning: A Laboratory Manual, J. Sambrook, et al., eds., Fourth Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 2012, or Current Protocols in Molecular Biology, F.M. Ausubel, et al., eds., John Wiley & Sons, Inc., New York. Conservative substitutions of amino acids include substitutions made amongst amino acids within the following groups: (a) M, I, L, V; (b) F, Y, W; (c) K, R, H; (d) A, G; (e) S, T; (f) Q, N; and (g) E, D.

[0049] Cross-reactive: As used herein and in the context of a targeting agent (e.g., antibody), the term “cross-reactive,” refers to a property of the agent being capable of specifically binding to more than one antigen of a similar type or class (e.g., antigens of multiple homologs, paralogs, or orthologs) with similar affinity or avidity. For example, in some embodiments, an antibody that is cross-reactive against human and non-human primate antigens of a similar type or class (e.g., a human TMPRSS6 and non-human primate TMPRSS6) is capable of binding to the human antigen and non-human primate antigens with a similar affinity or avidity. In some embodiments, an antibody is cross-reactive against a human antigen and a rodent antigen of a similar type or class. In some embodiments, an antibody is cross-reactive against a rodent antigen and a non-human primate antigen of a similar type or class. In some embodiments, an antibody is cross-reactive against a human antigen, a non-human primate antigen, and a rodent antigen of a similar type or class.11#14616800v2

[0050] Effective Amount: As used herein, “an effective amount” refers to the amount of each active agent (e.g., anti-TMPRSS6 antibody described herein) required to confer therapeutic effect on the subject, either alone or in combination with one or more other active agents. In some embodiments, the therapeutic effect comprises reduced TMPRSS6 level or activity, increased hepcidin level or activity, and / or alleviated disease conditions (e.g., iron overload in sickle cell disease, thalassemia, hemochromatosis, etc.).

[0051] Framework: As used herein, the term "framework" or "framework sequence" refers to the remaining amino acid residues of a variable region (e.g., VH or VL) minus the CDRs. Because the exact definition of a CDR sequence can be determined by different systems, the meaning of a framework sequence is subject to correspondingly different interpretations. The six CDRs (LC CDR, LC CDR, and LC CDR of a VL and HC CDR, HC CDR, and HC CDR of a VH) also divide the framework regions on the VL and the VH into four sub-regions (LC FR1, LC FR2, LC FR3, and LC FR4 of a VL, and HC FR1, HC FR2, HC FR3, and HC FR4 of a VH) on each chain. In each variable region, CDR1 is positioned between FR1 and FR2, CDR2 is positioned between FR2 and FR3, and CDR3 is positioned between FR3 and FR4. Without specifying the particular sub-regions as FR1, FR2, FR3 or FR4, a “framework region” represents the combined FRs within the variable region of a single, naturally occurring immunoglobulin chain. As used herein, “a FR” represents one of the four sub-regions, and “FRs” represents two or more of the four sub-regions constituting a framework region. Human heavy chain and light chain acceptor sequences are known in the art. In one embodiment, the acceptor sequences known in the art may be used in the antibodies disclosed herein. In some embodiments, the sequences of the disclosed framework regions may vary by up to 20% (e.g., the sequences are about 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to the disclosed sequence.

[0052] Human antibody: The term "human antibody", as used herein, includes antibodies having variable regions and constant regions derived from human germline immunoglobulin sequences. The human antibodies of the disclosure may include amino acid residues not encoded by human germline immunoglobulin sequences (e.g., mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo), for example in the CDRs, and in particular CDR3. However, the term "human antibody", as used herein, does not include CDR-grafted antibodies in which CDR sequences derived from the germline of another mammalian species, such as a mouse, have been grafted onto human framework sequences.12#14616800v2

[0053] Humanized antibody: The term "humanized antibody" refers to antibodies which comprise a VH and a VL from a non-human species (e.g., a mouse) in which at least a portion of the VH and / or VL sequence has been altered to be more "human-like", i.e., more similar to human germline variable sequences. One type of humanized antibody is a CDR- grafted antibody, in which human CDR sequences are introduced into non-human VH and VL sequences to replace the corresponding nonhuman CDR sequences. In one embodiment, humanized anti-TMPRSS6 antibodies and antigen binding portions thereof are provided. Such antibodies may be generated by obtaining murine anti-TMPRSS6 monoclonal antibodies using traditional hybridoma technology followed by humanization using in vitro genetic engineering, such as those disclosed in Kasaian et al PCT publication No. WO 2005 / 123126 A2.

[0054] In some embodiments, a humanized antibodies comprises a human immunoglobulin as a “recipient antibody” of CDRs of a non-human species of a “donor antibody”; for example, residues from a CDR of the recipient antibody can be replaced with residues from a corresponding CDR of a non-human donor antibody (e.g., mouse, rat, or rabbit antibody) having a desired specificity, affinity, and / or capacity. In some embodiments, Fv FR residues of the human immunoglobulin are also replaced by corresponding non-human residues. A humanized antibody may also comprise residues that are found neither in the recipient antibody nor in the imported CDR or framework sequences, but that are included to further refine and optimize antibody performance. In general, all or substantially all of the CDR regions of at least one (and typically two) variable domain in a humanized antibody correspond to those of the corresponding variable domain(s) of a donor antibody; and all or substantially all of the FR regions of the corresponding variable domain(s) of the humanized antibody are those of a human immunoglobulin consensus sequence. The humanized antibody optimally will also comprise at least a portion of an immunoglobulin constant region or domain (Fc), typically that of a human immunoglobulin. Antibodies may have Fc regions modified as described in WO 99 / 58572. In some embodiments, humanized antibodies comprise one or more CDRs (one, two, three, four, five, or six CDRs) which are altered with respect to the non-human donor antibody; these altered CDRs are also described as being “derived” from the donor antibody. Humanized antibodies may also involve affinity maturation

[0055] In some embodiments, humanization is achieved by grafting CDRs (e.g., defined as shown in Table 1) of a non-human donor antibody into the variable domain(s) of the human recipient antibody (e.g., IGKVl-NLl*01 and IGHVl-3*01 human variable domain).13#14616800v2In some embodiments, the anti-TMPRSS6 antibody of the present disclosure is a humanized variant comprising one or more amino acid substitutions (e.g., in the VH framework region) as compared with any one of the VHs listed in Table 1, and / or one or more amino acid substitutions (e.g., in the VL framework region) as compared with any one of the VLs listed in Table 1.

[0056] Isolated antibody: An "isolated antibody", as used herein, is intended to refer to an antibody that is substantially free of other antibodies having different antigenic specificities (e.g., an isolated antibody that specifically binds TMPRSS6 is substantially free of antibodies that specifically bind antigens other than TMPRSS6). An isolated antibody that specifically binds TMPRSS6 may, however, have cross-reactivity to other antigens. Moreover, an isolated antibody may be substantially free of other cellular material and / or chemicals.

[0057] Kabat numbering: The terms "Kabat numbering", "Kabat definitions and "Kabat labeling" are used interchangeably herein. These terms, which are recognized in the art, refer to a system of numbering amino acid residues which are more variable (i.e. hypervariable) than other amino acid residues in the heavy and light chain variable regions of an antibody, or an antigen binding portion thereof (Kabat et al. (1971) Ann. NY Acad, Sci. 190:382-391 and, Kabat, E. A., et al. (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242). For a VH, the hypervariable region ranges from amino acid positions 31 to 35 for HC CDR1, amino acid positions 50 to 65 for HC CDR2, and amino acid positions 95 to 102 for HC CDR3. For a VL, the hypervariable region ranges from amino acid positions 24 to 34 for LC CDR1, amino acid positions 50 to 56 for LC CDR2, and amino acid positions 89 to 97 for LC CDR3.

[0058] Percent (%) sequence identity: The terms “Percent (%) sequence identity”, “percent (%) identity”, and “percent (%) identity to” with respect to a reference polypeptide (or nucleotide) sequence is defined as the percentage of amino acid residues (or nucleic acids) in a candidate sequence that are identical to the amino acid residues (or nucleic acids) in the reference polypeptide (or nucleotide) sequence, after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity, and not considering any conservative substitutions as part of the sequence identity. Alignment for purposes of determining percent sequence identity can be achieved in various ways that are within the skill in the art, for instance, using publicly available computer software such as BLAST, BLAST-2, ALIGN or Megalign (DNASTAR) software. Those skilled in the art can determine appropriate parameters for aligning sequences, including any algorithms needed to14#14616800v2achieve maximal alignment over the full length of the sequences being compared. For purposes herein, however, % amino acid (or nucleic acid) sequence identity values are generated using the sequence comparison computer program ALIGN-2. The ALIGN-2 sequence comparison computer program was authored by Genentech, Inc., and the source code has been filed with user documentation in the U.S. Copyright Office, Washington D.C., 20559, where it is registered under U.S. Copyright Registration No. TXU510087. The ALIGN-2 program is publicly available from Genentech, Inc., South San Francisco, Calif., or may be compiled from the source code. The ALIGN-2 program should be compiled for use on a UNIX operating system, including digital UNIX V4.0D. All sequence comparison parameters are set by the ALIGN-2 program and do not vary.

[0059] Recombinant antibody: The term "recombinant antibody", as used herein, is intended to include all antibodies that are prepared, expressed, created, or isolated by recombinant means. In some embodiments, recombinant antibodies are antibodies expressed using a recombinant expression vector transfected into a host cell (e.g., as described herein), including, for example, antibodies isolated from a recombinant, combinatorial human antibody library (Hoogenboom H. R., (1997) TIB Tech. 15:62-70; Azzazy H., and Highsmith W. E., (2002) Clin. Biochem. 35:425-445; Gavilondo J. V., and Larrick J. W. (2002) BioTechniques 29: 128-145; Hoogenboom H., and Chames P. (2000) Immunology Today 21 :371-378). In some embodiments, a recombinant antibody is an antibody isolated from a transgenic animal e.g., a transgenic mouse) that has been engineered to express human immunoglobulin genes (see e.g., Taylor, L. D., et al. (1992) Nucl. Acids Res. 20:6287-6295; Kellermann S-A., and Green L. L. (2002) Current Opinion in Biotechnology 13:593-597; Little M. et al (2000) Immunology Today 21 :364-370). In some embodiments, a recombinant antibody is an antibody prepared, expressed, created, or isolated by any other means that involves splicing of human immunoglobulin gene sequences into other DNA sequences. In some embodiments, recombinant human antibodies are provided herein. In certain embodiments, such recombinant human antibodies have variable and constant regions derived from human germline immunoglobulins. In certain embodiments, however, such recombinant human antibodies are subjected to in vitro mutagenesis or in vivo somatic mutagenesis (e.g., when an animal transgenic for human Ig sequences is used); thus amino acid sequences of the VH and VL regions of such recombinant antibodies may be derived from and related to human germline VH and VL sequences, but may not naturally exist within the human antibody germline repertoire in vivo. One embodiment of the disclosure provides fully human antibodies capable of binding human TMPRSS6 which can be15#14616800v2generated using techniques well known in the art, such as, but not limited to, using human Ig phage libraries (e.g., as disclosed in Jermutus et al., PCT publication No. WO 2005 / 007699 A2).

[0060] Selective: As used herein, the term “selective” or “selectively” refers to an ability of a molecule to produce an effect (e.g., inhibit, antagonize, agonize, etc.) on a target molecule or cell to a degree that is distinguishable from its effect on a reference (e.g., nontarget) molecule or cell. For example, a molecule that “selectively inhibits” its target molecule is capable of inhibiting its target molecule with a degree that is distinguishable from an effect it may have on a reference molecule, e.g., in an inhibition assay or other inhibitory context. In some embodiments, a molecule that selectively inhibits a target molecule inhibits the target molecule and does not substantially inhibit one or more reference molecules (e.g., in an inhibition assay). In some embodiments, a molecule is determined to selectively inhibit a target molecule relative to a reference molecule via an inhibition assay, whereby, once the reaction is terminated, signals produced by inhibiting the target molecule can be measured, and the half maximal inhibitor concentration for the target molecule and the reference molecule can be calculated. In some embodiments, a molecule described herein selectively binds to a target molecule.

[0061] Specifically binds: As used herein, the term “specifically binds” refers to the ability of a molecule to bind to a binding partner with a degree of affinity or avidity that enables the molecule to be used to distinguish the binding partner from an appropriate control in a binding assay or other binding context. With respect to an antibody, the term, “specifically binds”, refers to the ability of the antibody to bind to a specific antigen with a degree of affinity or avidity, compared with an appropriate reference antigen or antigens, that enables the antibody to be used to distinguish the specific antigen from others, as described herein. In some embodiments, an antibody specifically binds to a target if the antibody has a KD for binding the target of at least about 10'4M, 10'5M, IO’6M, 10'7M, 10'8M, 10'9M, 10’10M, 10’11M, IO’12M, 10'13M, or less. In some embodiments, an antibody specifically binds TMPRSS6.

[0062] Subject: As used herein, the term “subject” refers to a mammal. In some embodiments, a subject is non-human primate, or rodent. In some embodiments, a subject is a human. In some embodiments, a subject is a patient, e.g., a human patient that has or is suspected of having a disease. In some embodiments, the subject is a human patient who has or is suspected of having iron overload and / or one or more conditions arising as a result of iron overload.16#14616800v2Treatment: As used herein, the term “treating”, “treated”, “treat” or “treatment” refers to the application or administration of a composition including one or more active agents (e.g., anti- TMPRSS6 antibodies described herein) to a subject, who has a target disease or disorder, a symptom of the disease / disorder, or a predisposition toward the disease / disorder, with the purpose to cure, heal, alleviate, relieve, alter, remedy, ameliorate, improve, or affect the disorder, the symptom of the disease, or the predisposition toward the disease or disorder. Alleviating a target disease / disorder includes delaying or preventing the onset, development or progression of the disease, or reducing disease severity. In some embodiments, the target disease or disorder of the present disclosure include but are not limited to hemochromatosis, sickle cell disease (SCD), thalassemia, hemolysis, African iron overload, Diamond-Blackfan anemia, myelodysplastic syndrome (MDS), and blood transfusion.II. Antibody formulation

[0063] Aspects of the present disclosure relate to compositions comprising an antibody (e.g., a stress-sensitive antibody), wherein the composition is formulated to promote resistance of the antibody to one or more stress conditions (e.g., light, thermal, and / or agitation stress. In some embodiments, a composition comprising a stress-sensitive antibody is formulated with components in amount effective to promote resistance of the antibody to one or more stress conditions (e.g., light, thermal, and / or agitation stress).

[0064] In some embodiments, compositions provided herein promote stability of an antibody under one or more stress conditions (e.g., light, thermal, and / or agitation stress). “Stability”, as used herein, refers to resistance of an antibody to structural and / or functional changes. In some embodiments, stability of an antibody is physical stability. In some embodiments, physical stability of an antibody refers to resistance of an antibody to physical changes, such as degradation and / or aggregation. In some embodiments, stability of an antibody is chemical stability. In some embodiments, chemical stability of an antibody refers to resistance of the antibody to chemical changes, such as post-translational modifications (PTMs). In some embodiments, stability of an antibody is functional stability. In some embodiments, functional stability of an antibody refers to resistance of the antibody to changes in function, such as changes in binding properties to its target antigen.

[0065] A “stress-sensitive antibody”, as used herein, refers to an antibody that is susceptible to certain stress conditions in the absence of mitigating factors (e.g., compositions provided), such that when exposed to one or more stress conditions, the antibody tends to17#14616800v2change in structure (e.g., via degradation, aggregation, and / or post translational modification) and / or function (e.g., via changes in antigen-binding properties) as compared to an antibody that is not stress-sensitive . In some embodiments, a stress-sensitive antibody is degraded when subjected to a stress condition. In some embodiments, a stress-sensitive antibody aggregates when subjected to a stress condition. In some embodiments, certain amino acids of the stress-sensitive antibody undergo post translational modifications (PTMs) (e.g., oxidation, di-oxidation) when exposed (e.g., subjected) to a stress condition. In some embodiments, an antigen-binding property (e.g., affinity, specificity) of a stress-sensitive antibody changes when exposed (e.g., subjected) to a stress condition. In some embodiments, exposing a stress-sensitive antibody to a stress condition decreases therapeutic effects of the antibody.Illustrative Stress Conditions

[0066] A “stress condition” or “stressor”, used interchangeably herein, refers to a condition that causes structural and / or functional changes to a stress-sensitive antibody. In some embodiments, a stress condition is a natural condition (e.g., sunlight). In some embodiments, a stress condition is a man-made condition (e.g., thermal, agitation, and / or light stress during antibody manufacturing, storage, handling, and / or transportation). Sensitivity of a stress-sensitive antibody to a particular stress condition may vary. For example, in some embodiments, a stress-sensitive antibody is sensitive to a first stress condition but not to a second stress condition. In another example, a stress-sensitive antibody is sensitive to multiple stress conditions, but is more sensitive to a first stress condition than to a second stress condition.Light Stress

[0067] In some embodiments, a stress condition comprises light stress. In some embodiments, a stress-sensitive antibody is sensitive to a light stressor (i.e., is a “lightsensitive antibody”). Exposure of proteins, such as antibodies, to light is associated with protein breakdown; for example, certain amino acids (e.g., tryptophan, tyrosine, phenylalanine, histidine) and peptide bonds (e.g., disulfide bonds) are known to be especially photosensitive, and exposure of proteins containing the same to light stress can result in aggregation and / or degradation. In some embodiments, tryptophan, tyrosine, phenylalanine, or histidine of light-sensitive antibodies is oxidized (e.g., di-oxidized) after exposure of the stress-sensitive antibody to light.18#14616800v2

[0068] In some embodiments, sensitivity of a stress-sensitive antibody to light depends on light wavelength, intensity, illuminance, and / or duration of exposure to a light stressor. As used herein, the term “light wavelength” refers to the spatial period of electromagnetic radiation (e.g., the distance from peak to trough of a photon); light wavelengths are typically measured in nanometers (nm). Light may be of any wavelength; for example, in some embodiments, light is visible light or ultraviolet light. Visible light encompasses the portion of the electromagnetic spectrum that is considered detectable by the human eye (e.g., about 380nm to 750nm). Ultraviolet (UV) light encompasses the portion of the electromagnetic spectrum containing wavelengths shorter than those of visible light, but longer than X-rays (e.g., about lOnm to about 400nm). In some embodiments, light is infrared (e.g., having a wavelength of about 750 nm to about 1000 nm). In some embodiments, light stress comprises mixtures of visible light, UV light, and / or infrared light; for example, numerous light sources (e.g., lightbulbs, light emitting diodes, sunlight) are known to comprise light having a variety of wavelengths.

[0069] As used herein, the term “intensity” refers to the total power emitted by a source per unit solid angle and is measured in watts per square meter (W / m2). “Light intensity” is an absolute measure of the amount of light energy emitted in all directions from a light source. In some embodiments, intensity is provided as intensity per hour, i.e., as W-h / m2. W-h / m2 can be determined from a given time period and intensity by multiplying the time in hours and the intensity in W / m2; for example, exposure to 10W / m2for 10 hours is 100 W-h / m2. As used herein, the term “illuminance” refers to the amount of visible light that falls onto a surface (e.g., an antibody surface) and is measured in lux. Illuminance depends on both the intensity of the light source and the distance from the source to the surface (e.g., from a light source to an antibody). In some embodiments, illuminance is provided as lux per hour, i.e., as “lux hours”. “Lux hours” refer to the total amount of illuminance (e.g., as measured in lux) per hour; lux hours can be determined from a given time period and illuminance by multiplying the time in hours and the illuminance in lux; for example, exposure to 1000 lux for 10 hours can also be referred to “10,000 lux hours”.

[0070] In some embodiments, a stress condition comprises a visible light stressor. In some embodiments, a visible light stressor comprises visible light (e.g., light having a wavelength of about 380nm to about 750nm) having an illuminance of at least 500 lux, at least 550 lux, at least 600 lux, at least 650 lux, at least 700 lux, at least 750 lux, at least 800 lux, at least 850 lux, at least 900 lux, at least 950 lux, at least 1000 lux, at least 1100 lux, at least 1200 lux, at least 1300 lux, at least 1400 lux, at least 1500 lux, at least 1600 lux, at least 1700 lux, at least 19#14616800v21800 lux, at least 1900 lux, at least 2000 lux, at least 2200 lux, at least 2400 lux, at least 2600 lux, at least 2800 lux, at least 3000 lux, at least 3250 lux, at least 3500 lux, at least 3750 lux, at least 4000 lux, at least 4250 lux, at least 4500 lux, at least 4750 lux, at least 5000 lux, at least 5500 lux, at least 6000 lux, at least 6500 lux, at least 7000 lux, at least 7500 lux, at least 8000 lux, at least 8500 lux, at least 9000 lux, at least 9500 lux, at least 10,000 lux, at least 11,000 lux, at least 12,000 lux, at least 13,000 lux, at least 14,000 lux, at least 15,000 lux, at least 16,000 lux, at least 17,000 lux, at least 18,000 lux, at least 19,000 lux, at least 20,000 lux, at least 22,00 lux, at least 24,000 lux, or at least 25,000 lux. In some embodiments, a stress-sensitive antibody that is sensitive to light is sensitive to visible light (e.g., light having a wavelength of about 380nm to about 750nm) having an intensity in the range of 500-25,000 lux, 1000-25,000 lux, 2000-25,000 lux, 3000-25,000 lux, 4000-25,000 lux, 5000-25,000 lux, 6000-25,000 lux, 7000-25,000 lux, 8000-25,000 lux, 9000-25,000 lux, 10,000-25,000 lux, 11,000-25,000 lux, 12,000-25,000 lux, 13,000-25,000 lux, 14,000-25,000 lux, 15,000-25,000 lux, 16,000-25,000 lux, 17,000-25,000 lux, 18,000-25,000 lux, 19,000-25,000 lux, 20, GOO- 25, 000 lux, 21,000-25,000 lux, 22,000-25,000 lux, 23,000-25,000 lux, 24,000-25,000 lux, 500-1000 lux, 500-2000 lux, 500-3000 lux, 500-4000 lux, 500-5000 lux, 500-6000 lux, 500- 7000 lux, 500-8000 lux, 500-9000 lux, 500-10,000 lux, 500-11,000 lux, 500-12,000 lux, SOO- 13, 000 lux, 500-14,000 lux, 500-15,000 lux, 500-16,000 lux, 500-17,000 lux, 500-18,000 lux, 500-19,000 lux, 500-20,000 lux, 500-21,000 lux, 500-22,000 lux, 500-23,000 lux, SOO- 24, 000 lux, 1000-2000 lux, 2000-3000 lux, 3000-4000 lux, 4000-5000 lux, 5000-6000 lux, 6000-7000 lux, 7000-8000 lux, 8000-9000 lux, 9000-10,000 lux, 10,000-11,000 lux, 11, GOO- 12, 000 lux, 12,000-13,000 lux, 13,000-14,000 lux, 14,000-15,000 lux, 15,000-16,000 lux, 16,000-17,000 lux, 17,000-18,000 lux, 18,000-19,000 lux, 20,000-21,000 lux, 21,000-22,000 lux, 22,000-23,000 lux, 23,000-24,000 lux, or 24,000-25,000 lux.

[0071] In some embodiments, a visible light stressor comprises visible light having a wavelength of between about 380 nm to about 750 nm, e.g., about 380 nm, about 400 nm, about 425 nm, about 450 nm, about 475 nm, about 500 nm, about 550 nm, about 600 nm, about 650 nm, about 700 nm, or about 750 nm. In some embodiments, a stress-sensitive antibody that is sensitive to light is sensitive to visible light having a wavelength in the range of 380-750 nm, 390-750 nm, 400-750 nm, 425-750nm, 450-750 nm, 475-750 nm, 500-750 nm, 550-750 nm, 600-750 nm, 650-750 nm, 700-750 nm, 380-400 nm, 380-425 nm, 380-450 nm, 380-475 nm, 380-500 nm, 380-550 nm, 380-600 nm, 380-650 nm, 380-700 nm, 380-750 nm, , 400-425 nm, 425-450 nm, 450-475 nm, 475-500 nm, 300-350 nm, 350-400 nm, 400- 450 nm, 450-500 nm, 500-550 nm, 550-600 nm, 600-650 nm, 650-700 nm, or 700-750 nm.20#14616800v2

[0072] In some embodiments, a stress condition comprises a UV light stressor. In some embodiments, a UV light stressor comprises UV light having a wavelength of between about 10 nm to about 400 nm. In some embodiments, a UV light stressor comprises UV light having a wavelength between about 315 nm to about 400 nm, e.g., about 315 nm, about 325 nm, about 350 nm, about 375 nm, or about 400 nm. In some embodiments, a stress-sensitive antibody that is sensitive to light is sensitive to UV light having a wavelength in the range of 315-325 nm, 315-350 nm, 315-375 nm, 315-400 nm, 325-350 nm, 350-375 nm, or 375-400 nm.

[0073] In some embodiments, a UV light stressor comprises UV light having an intensity of at least 1 W / m2, at least 2 W / m2, at least 3 W / m2, at least 4 W / m2, at least 5 W / m2, at least 6 W / m2, at least 7 W / m2, at least 8 W / m2, at least 9 W / m2, at least 10 W / m2, at least 11 W / m2, at least 12 W / m2, at least 13 W / m2, at least 14 W / m2, at least 15 W / m2, at least 16 W / m2, at least 17 W / m2, at least 18 W / m2, at least 19 W / m2, or at least 20 W / m2. In some embodiments, a stress-sensitive antibody that is sensitive to light is sensitive to UV light having an intensity in the range of 1-20 W / m2, 2-20 W / m2, 3-20 W / m2, 4-20 W / m2, 5-20 W / m2, 6-20 W / m2, 7-20 W / m2, 8-20 W / m2, 9-20 W / m2, 10-20 W / m2, 11-20 W / m2, 12-20 W / m2, 13-20 W / m2, 14-20 W / m2, 15-20 W / m2, 16-20 W / m2, 17-20 W / m2, 18-20 W / m2, 19- 20 W / m2, 1-2 W / m2, 1-3 W / m2, 1-4 W / m2, 1-5 W / m2, 1-6 W / m2, 1-7 W / m2, 1-8 W / m2, 1-9 W / m2, 1-10 W / m2, 1-11 W / m2, 1-12 W / m2, 1-13 W / m2, 1-14 W / m2, 1-15 W / m2, 1-16 W / m2, 1-17 W / m2, 1-18 W / m2, 1-19 W / m2, 2-3 W / m2, 3-4 W / m2, 4-5 W / m2, 5-6 W / m2, 6-7 W / m2, 7-8 W / m2, 8-9 W / m2, 9-10 W / m2, 10-11 W / m2, 11-12 W / m2, 12-13 W / m2, 13-14 W / m2, 14- 15 W / m2, 15-16 W / m2, 16-17 W / m2, 17-18 W / m2, or 18-10 W / m2.

[0074] In some embodiments, a stress condition comprises an infrared light stressor. In some embodiments, a visible light stressor comprises infrared light (e.g., light having a wavelength of about 750 nm to about 1000 nm) having an illuminance of at least 500 lux, at least 550 lux, at least 600 lux, at least 650 lux, at least 700 lux, at least 750 lux, at least 800 lux, at least 850 lux, at least 900 lux, at least 950 lux, at least 1000 lux, at least 1100 lux, at least 1200 lux, at least 1300 lux, at least 1400 lux, at least 1500 lux, at least 1600 lux, at least 1700 lux, at least 1800 lux, at least 1900 lux, at least 2000 lux, at least 2200 lux, at least 2400 lux, at least 2600 lux, at least 2800 lux, at least 3000 lux, at least 3250 lux, at least 3500 lux, at least 3750 lux, at least 4000 lux, at least 4250 lux, at least 4500 lux, at least 4750 lux, at least 5000 lux, at least 5500 lux, at least 6000 lux, at least 6500 lux, at least 7000 lux, at least 7500 lux, at least 8000 lux, at least 8500 lux, at least 9000 lux, at least 9500 lux, at least10,000 lux, at least 11,000 lux, at least 12,000 lux, at least 13,000 lux, at least 14,000 lux, at21#14616800v2least 15,000 lux, at least 16,000 lux, at least 17,000 lux, at least 18,000 lux, at least 19,000 lux, at least 20,000 lux, at least 22,00 lux, at least 24,000 lux, or at least 25,000 lux. In some embodiments, a stress-sensitive antibody that is sensitive to light is sensitive to infrared light (e.g., light having a wavelength of about 750 nm to about 1000 nm) having an intensity in the range of 500-25,000 lux, 1000-25,000 lux, 2000-25,000 lux, 3000-25,000 lux, 4000-25,000 lux, 5000-25,000 lux, 6000-25,000 lux, 7000-25,000 lux, 8000-25,000 lux, 9000-25,000 lux, 10,000-25,000 lux, 11,000-25,000 lux, 12,000-25,000 lux, 13,000-25,000 lux, 14,000-25,000 lux, 15,000-25,000 lux, 16,000-25,000 lux, 17,000-25,000 lux, 18,000-25,000 lux, 19, GOO- 25, 000 lux, 20,000-25,000 lux, 21,000-25,000 lux, 22,000-25,000 lux, 23,000-25,000 lux, 24,000-25,000 lux, 500-1000 lux, 500-2000 lux, 500-3000 lux, 500-4000 lux, 500-5000 lux, 500-6000 lux, 500-7000 lux, 500-8000 lux, 500-9000 lux, 500-10,000 lux, 500-11,000 lux, 500-12,000 lux, 500-13,000 lux, 500-14,000 lux, 500-15,000 lux, 500-16,000 lux, SOO- 17, 000 lux, 500-18,000 lux, 500-19,000 lux, 500-20,000 lux, 500-21,000 lux, 500-22,000 lux, 500-23,000 lux, 500-24,000 lux, 1000-2000 lux, 2000-3000 lux, 3000-4000 lux, 4000-5000 lux, 5000-6000 lux, 6000-7000 lux, 7000-8000 lux, 8000-9000 lux, 9000-10,000 lux, 10,000- 11,000 lux, 11,000-12,000 lux, 12,000-13,000 lux, 13,000-14,000 lux, 14,000-15,000 lux, 15,000-16,000 lux, 16,000-17,000 lux, 17,000-18,000 lux, 18,000-19,000 lux, 20,000-21,000 lux, 21,000-22,000 lux, 22,000-23,000 lux, 23,000-24,000 lux, or 24,000-25,000 lux.

[0075] In some embodiments, an infrared light stressor comprises infrared light having a wavelength of between about 750 nm to about 1000 nm, e.g., about 750 nm, about 775 nm, about 800 nm, about 825 nm, about 850 nm, about 875 nm, about 900 nm, about 925 nm, about 950 nm, about 975 nm, or about 1000 nm. In some embodiments, a stress-sensitive antibody that is sensitive to light is sensitive to visible light having a wavelength in the range of 750-1000 nm, 800-1000 nm, 850-1000nm, 900-1000 nm, 950-1000 nm, 750-950 nm, 800- 950 nm, 850-950nm, 900-950 nm, 750-900 nm, 800-900 nm, 850-900nm, 750-850 nm, 760- 850 nm, 770-850 nm, 780-850 nm, 790-850 nm, 800-850 nm, 810-850 nm, 820-850 nm, 830- 850 nm, 840-850 nm, 750-825 nm, 760-825 nm, 770-825 nm, 780-825 nm, 790-825 nm, 800- 825nm, 810-825 nm, 820-825 nm, 750-800 nm, 760-800 nm, 770-800 nm, 780-800 nm, or 790-800 nm.

[0076] In some embodiments, light stress comprises exposure to visible light having an illuminance of at least 3000 lux and / or having a wavelength in the range of 380-750 nm for no more than 15 days. In some embodiments, light stress comprises exposure to visible light having an illuminance of at least 300 lux and / or having a wavelength in the range of 380-750 nm for at least 5 days, at least 6 days, at least 7 days, at least 8 days, at least 9 days, at least 22#14616800v210 days, at least 11 days, at least 12 days, at least 13 days, at least 14 days, or at least 15 days. In some embodiments, light stress comprises exposure to visible light having an illuminance of at least 3000 lux and / or having a wavelength in the range of 380-750 nm for a time period in the range of 5-15 days, 6-15 days, 7-15 days, 8-15 days, 9-15 days, 10-15 days, 11-15 days, 12-15 days, 13-15 days, 14-15 days, 5-6 days, 5-7 days, 5-8 days, 5-9 days, 5-10 days, 5-11 days, 5-12 days, 5-13 days, 5-14 days, 6-7 days, 7-8 days, 8-9 days, 9-10 days, 10-11 days, 11-12 days, 12-13 days, or 13-14 days.

[0077] In some embodiments, light stress comprises exposure to infrared light having an illuminance of at least 3000 lux and / or having a wavelength in the range of 750-800 nm for no more than 15 days. In some embodiments, light stress comprises exposure to infrared light having an illuminance of at least 300 lux and / or having a wavelength in the range of 750-800 nm for at least 5 days, at least 6 days, at least 7 days, at least 8 days, at least 9 days, at least 10 days, at least 11 days, at least 12 days, at least 13 days, at least 14 days, or at least 15 days. In some embodiments, light stress comprises exposure to infrared light having an illuminance of at least 3000 lux and / or having a wavelength in the range of 750-800 nm for a time period in the range of 5-15 days, 6-15 days, 7-15 days, 8-15 days, 9-15 days, 10-15 days, 11-15 days, 12-15 days, 13-15 days, 14-15 days, 5-6 days, 5-7 days, 5-8 days, 5-9 days, 5-10 days, 5-11 days, 5-12 days, 5-13 days, 5-14 days, 6-7 days, 7-8 days, 8-9 days, 9-10 days, 10-11 days, 11-12 days, 12-13 days, or 13-14 days.

[0078] In some embodiments, light stress comprises exposure to UV light (e.g., light having a wavelength of 315-400 nm) having an intensity of 4 W / m2for no more than 50 hours. In some embodiments, light stress comprises exposure to UV light (e.g., light having a wavelength of 315-400 nm) having an intensity of 4 W / m2for at least 12 hours, at least 13 hours, at least 14 hours, at least 15 hours, at least 16 hours, at least 17 hours, at least 18 hours, at least 19 hours, at least 20 hours, at least 22 hours, at least 24 hours, at least 26 hours, at least 28 hours, at least 30 hours, at least 32.5 hours, at least 35 hours, at least 37.5 hours, at least 40 hours, at least 42.5 hours, at least 45 hours, at least 47.5 hours, at least 50 hours, at least 55 hours, at least 60 hours, at least 65 hours, at least 70 hours, or at least 75 hours. In some embodiments, light stress comprises exposure to UV light (e.g., light having a wavelength of 315-400 nm) having an intensity of 4 W / m2for a time period in the range of 12-75 hours, 13-75 hours, 14-75 hours, 15-75 hours, 16-75 hours, 17-75 hours, 18-75 hours, 19-75 hours, 20-75 hours, 22-75 hours, 24-75 hours, 26-75 hours, 28-75 hours, 30-75 hours, 32.5-75 hours, 35-75 hours, 37.5-75 hours, 40-75 hours, 42.5-75 hours, 45-75 hours, 47.5-75 hours, 50-75 hours, 55-75 hours, 60-75 hours, 65-70 hours, 70-75 hours, 12-13 hours, 12-14 23#14616800v2hours, 12-15 hours, 12-16 hours, 12-17 hours, 12-18 hours, 12-19 hours, 12-20 hours, 12-22 hours, 12-24 hours, 12-26 hours, 12-28 hours, 12-30 hours, 12-32.5 hours, 12-35 hours, 12-37.5 hours, 12-40 hours, 12-42.5 hours, 12-45 hours, 12-47.5 hours, 12-50 hours, 12-55 hours, 12-60 hours, 12-65 hours, 12-70 hours, 13-14 hours, 14-15 hours, 15-16 hours, 16-17 hours, 17-18 hours, 18-19 hours, 19-20 hours, 20-22 hours, 22-24 hours, 24-26 hours, 26-28 hours, 28-30 hours, 30-32.5 hours, 32.5-35 hours, 35-37.5 hours, 37.5-40 hours, 40-42.5 hours, 42.5-45 hours, 45-47.5 hours, 47.5-50 hours, 50-55 hours, 55-60 hours, 60-65 hours, or 65-70 hours.

[0079] In some embodiments, light stress comprises exposure to visible light having an illuminance of at least 3000 lux and / or having a wavelength in the range of 380-750 nm for a time period in the range of 5-15 days, 6-15 days, 7-15 days, 8-15 days, 9-15 days, 10-15 days, 11-15 days, 12-15 days, 13-15 days, 14-15 days, 5-6 days, 5-7 days, 5-8 days, 5-9 days, 5-10 days, 5-11 days, 5-12 days, 5-13 days, 5-14 days, 6-7 days, 7-8 days, 8-9 days, 9-10 days, 10-11 days, 11-12 days, 12-13 days, or 13-14 days, and followed by being exposed to UV light (e.g., light having a wavelength of 315-400 nm) having an intensity of 4 W / m2for a time period in the range of 12-75 hours, 13-75 hours, 14-75 hours, 15-75 hours, 16-75 hours, 17-75 hours, 18-75 hours, 19-75 hours, 20-75 hours, 22-75 hours, 24-75 hours, 26-75 hours, 28-75 hours, 30-75 hours, 32.5-75 hours, 35-75 hours, 37.5-75 hours, 40-75 hours, 42.5-75 hours, 45-75 hours, 47.5-75 hours, 50-75 hours, 55-75 hours, 60-75 hours, 65-70 hours, 70- 75 hours, 12-13 hours, 12-14 hours, 12-15 hours, 12-16 hours, 12-17 hours, 12-18 hours, 12- 19 hours, 12-20 hours, 12-22 hours, 12-24 hours, 12-26 hours, 12-28 hours, 12-30 hours, 12-32.5 hours, 12-35 hours, 12-37.5 hours, 12-40 hours, 12-42.5 hours, 12-45 hours, 12-47.5 hours, 12-50 hours, 12-55 hours, 12-60 hours, 12-65 hours, 12-70 hours, 13-14 hours, 14-15 hours, 15-16 hours, 16-17 hours, 17-18 hours, 18-19 hours, 19-20 hours, 20-22 hours, 22-24 hours, 24-26 hours, 26-28 hours, 28-30 hours, 30-32.5 hours, 32.5-35 hours, 35-37.5 hours, 37.5-40 hours, 40-42.5 hours, 42.5-45 hours, 45-47.5 hours, 47.5-50 hours, 50-55 hours, 55- 60 hours, 60-65 hours, or 65-70 hours.

[0080] In some embodiments, light stress comprises exposure to infrared light having an illuminance of at least 3000 lux and / or having a wavelength in the range of 750-800 nm for a time period in the range of 5-15 days, 6-15 days, 7-15 days, 8-15 days, 9-15 days, 10-15 days, 11-15 days, 12-15 days, 13-15 days, 14-15 days, 5-6 days, 5-7 days, 5-8 days, 5-9 days, 5-10 days, 5-11 days, 5-12 days, 5-13 days, 5-14 days, 6-7 days, 7-8 days, 8-9 days, 9-10 days, 10-11 days, 11-12 days, 12-13 days, or 13-14 days, and followed by being exposed to UV light (e.g., light having a wavelength of 315-400 nm) having an intensity of 4 W / m2for a 24#14616800v2time period in the range of 12-75 hours, 13-75 hours, 14-75 hours, 15-75 hours, 16-75 hours, 17-75 hours, 18-75 hours, 19-75 hours, 20-75 hours, 22-75 hours, 24-75 hours, 26-75 hours, 28-75 hours, 30-75 hours, 32.5-75 hours, 35-75 hours, 37.5-75 hours, 40-75 hours, 42.5-75 hours, 45-75 hours, 47.5-75 hours, 50-75 hours, 55-75 hours, 60-75 hours, 65-70 hours, 70- 75 hours, 12-13 hours, 12-14 hours, 12-15 hours, 12-16 hours, 12-17 hours, 12-18 hours, 12- 19 hours, 12-20 hours, 12-22 hours, 12-24 hours, 12-26 hours, 12-28 hours, 12-30 hours, 12- 32.5 hours, 12-35 hours, 12-37.5 hours, 12-40 hours, 12-42.5 hours, 12-45 hours, 12-47.5 hours, 12-50 hours, 12-55 hours, 12-60 hours, 12-65 hours, 12-70 hours, 13-14 hours, 14-15 hours, 15-16 hours, 16-17 hours, 17-18 hours, 18-19 hours, 19-20 hours, 20-22 hours, 22-24 hours, 24-26 hours, 26-28 hours, 28-30 hours, 30-32.5 hours, 32.5-35 hours, 35-37.5 hours, 37.5-40 hours, 40-42.5 hours, 42.5-45 hours, 45-47.5 hours, 47.5-50 hours, 50-55 hours, 55- 60 hours, 60-65 hours, or 65-70 hours.

[0081] In some embodiments, a stress condition comprises exposure to any of the visible light stressors described herein for any of the time period described herein, any of the infrared light stressors described herein for any of the time period described herein, and / or any of the UV light stressors described herein for any of the time period described herein. In some embodiments, a stress condition comprises exposure to visible light having an illuminance of 5000 lux for 10 days. In some embodiments, a stress condition comprises exposure to UV light having an intensity of 4 W / m2for 50 hours. In some embodiments, a stress condition comprises exposure to visible light having an illuminance of 5000 lux for 10 days followed by being exposed to UV light having an intensity of 4 W / m2for 50 hours.Thermal Stress

[0082] In some embodiments, a stress condition comprises thermal stress (e.g., heat). In some embodiments, a stress-sensitive antibody is sensitive to a thermal stressor (i.e., is a “temperature-sensitive antibody”). Exposure of proteins to thermal stress is associated with protein breakdown and / or loss of function. For example, exposure to heat may denature antibodies, which may in turn lead to structural changes (e.g., destruction of peptide bonds, loss of three-dimensional structure), functional defects (e.g., reduction in binding activity and / or specificity), and protein aggregation. Exposure to freeze-thaw cycles may lead formation of ice crystals and / or phase separation of solutes in a solution, which may in turn lead to oxidative stress, disruption of protein structure (e.g., due to osmotic imbalance, exposure of hydrophobic cores to water, interactions with crystallized solute forms), functional defects, and protein instability.25#14616800v2

[0083] In some embodiments, sensitivity of a stress-sensitive antibody to thermal stress depends on the temperature and / or duration of exposure to thermal stress (e.g., heat). In some embodiments, a thermal stressor comprises an elevated temperature, i.e., a temperature at or above about 35 °C. In some embodiments, a stress-sensitive antibody sensitive to a thermal stressor is sensitive to elevated temperatures. In some embodiments, a thermal stressor comprises freezing and / or thawing processes (e.g., freeze-thaw stress). As used herein, “freeze-thaw” refers to a process in which a composition is frozen and subsequently thawed. Freeze-thaw cycles are often used for the storage and preservation of biological compositions (e.g., antibodies), wherein a composition is frozen to preserve its integrity and subsequently thawed to use said composition for analysis or for use. In some embodiments, a stresssensitive antibody sensitive to a thermal stressor is sensitive to freezing and / or thawing processes (e.g., freeze-thaw cycles).

[0084] In some embodiments, a thermal stressor comprises a temperature of at least 35 °C, at least 36°C, at least 37°C, at least 38°C, at least 39°C, at least 40°C, at least 42.5°C, at least 45°C, at least 47.5°C, at least 50°C, at least 55°C, at least 60°C, at least 65°C, at least 70°C, at least 75°C, at least 80°C, at least 85°C, at least 90°C, or at least 100°C. In some embodiments, a stress-sensitive antibody that is sensitive to thermal stress is sensitive to a temperature in the range of 35-100°C, 37.5-100°C, 40-100°C, 42.5-100°C, 45-100°C, 47.5- 100°C, 50-100°C, 55-100°C, 60-100°C, 65-100°C, 70-100°C, 75-100°C, 80-100°C, 85- 100°C, 90-100°C, 95-100°C, 35-37.5°C, 35-40°C, 35-42.5°C, 35-45°C, 35-47.5°C, 35-50°C, 35-55°C, 35-60°C, 35-65°C, 35-70°C, 35-75°C, 35-80°C, 35-85°C, 35-90°C, 35-95°C, 37.5- 40°C, 40-42.5°C, 42.5-45°C, 45-47.5°C, 47.5-50°C, 50-55°C, 55-60°C, 60-65°C, 65-70°C, 70-75°C, 75-80°C, 80-85°C, 85-90°C, or 90-95°C.

[0085] In some embodiments, thermal stress comprises exposure to an elevated temperature (e.g., 40°C) for at least 1 day, at least 2 days, at least 3 days, at least 4 days, at least 5 days, at least 6 days, at least 7 days, at least 8 days, at least 9 days, at least 10 days, at least 11 days, at least 12 days, at least 13 days, at least 14 days, at least 15 days, at least 16 days, at least 17 days, at least 18 days, at least 19 days, at least 20 days, at least 22 days, at least 24 days, at least 26 days, at least 28 days, or at least 30 days. In some embodiments, thermal stress comprises exposure to an elevated temperature (e.g., 40°C) for a time period in the range of 1-30 days, 2-30 days, 3-30 days, 4-30 days, 5-30 days, 6-30 days, 7-30 days, 8- 30 days, 9-30 days, 10-30 days, 11-30 days, 12-30 days, 13-30 days, 14-30 days, 15-30 days, 16-30 days, 17-30 days, 18-30 days, 19-30 days, 20-30 days, 22-30 days, 24-30 days, 26-30 days, 28-30 days, 1-2 days, 1-3 days, 1-4 days, 1-5 days, 1-6 days, 1-7 days, 1-8 days, 1-9 26#14616800v2days, 1-10 days, 1-11 days, 1-12 days, 1-13 days, 1-14 days, 1-15 days, 1-16 days, 1-17 days, 1-18 days, 1-19 days, 1-20 days, 1-22 days, 1-24 days, 1-26 days, 1-28 days, 2-3 days, 3-4 days, 4-5 days, 5-6 days, 6-7 days, 7-8 days, 8-9 days, 9-10 days, 10-11 days, 11-12 days, 12- 13 days, 13-14 days, 14-15 days, 15-16 days, 16-17 days, 17-18 days, 18-19 days, 19-20 days, 20-22 days, 22-24 days, 24-26 days, or 26-28 days.

[0086] In some embodiments, a thermal stressor comprises a freeze-thaw cycle. In some embodiments, a thermal stressor comprises a plurality of freeze-thaw cycles. In some embodiments, a thermal stressor comprises at least 1 freeze-thaw cycle, at least 2 freeze-thaw cycles, at least 3 freeze-thaw cycles, at least 4 freeze-thaw cycles, at least 5 freeze-thaw cycles, at least 6 freeze-thaw cycles, at least 7 freeze-thaw cycles, at least 8 freeze-thaw cycles, at least 9 freeze-thaw cycles, or at least 10 freeze-thaw cycles. In some embodiments, a stress-sensitive antibody sensitive to thermal stress is sensitive to a freeze-thaw cycle performed in the range of 1-10 times, 2-10 times, 3-10 times, 4-10 times, 5-10 times, 6-10 times, 7-10 times, 8-10 times, 9-10 times, 1-2 times, 1-3 times, 1-4 times, 1-5 times, 1-6 times, 1-7 times, 1-8 times, 1-9 times, 2-3 times, 3-4 times, 4-5 times, 5-6 times, 6-7 times, 7- 8 times, or 8-9 times.Agitation Stress

[0087] In some embodiments, a stress condition comprises agitation stress. In some embodiments, a stress-sensitive antibody is sensitive to an agitation stressor (i.e., is an “agitation-sensitive antibody”).

[0088] In some embodiments, sensitivity of a stress-sensitive antibody to agitation stress depends on agitation speed and / or duration of exposure to agitation. As used herein, “agitation” refers to movement beyond that which is expected in the normal storage, handling, and / or transport of a composition. In some embodiments, agitation comprises repetitive movements, such as shaking or spinning. In some embodiments, agitative movements are rapid. Agitation can contribute to the breakdown of antibodies through mechanical stress, shear force, introduction of air-liquid interfaces, enhanced temperature (e.g., thermal stress), and / or oxidative stress. In some embodiments, an antibody is sensitive to agitation when subjected to mechanical stress and / or shear force, which may lead to unfolding or denaturation of the antibody. In some embodiments, agitation introduces air into liquid solutions, creating air-liquid interfaces. In some embodiments, an antibody adsorbed into an air-liquid interface undergoes structural changes or denaturation. In some embodiments, agitation increases the temperature of a composition due to frictional heating,27#14616800v2which, in some embodiments, accelerates protein degradation (e.g., aggregation or fragmentation of the antibody). In some embodiments, agitation increases the transfer of oxygen into a composition, leading to increased oxidative stress of an antibody.

[0089] In some embodiments, a stress condition comprises spinning (e.g., rotation) agitation stress. In some embodiments, an agitation stressor comprises spinning (e.g., rotating) at a speed in the range of 100-1000 rpm, 110-1000 rpm, 120-1000 rpm, 130-1000 rpm, 140-1000 rpm, 150-1000 rpm, 160-1000 rpm, 170-1000 rpm, 180-1000 rpm, 190-1000 rpm, 200-1000 rpm, 220-1000 rpm, 240-1000 rpm, 260-1000 rpm, 280-1000 rpm, 300-1000 rpm, 325-1000 rpm, 350-1000 rpm, 375-1000 rpm, 400-1000 rpm, 425-1000 rpm, 450-1000 rpm, 475-1000 rpm, 500-1000 rpm, 550-1000 rpm, 600-1000 rpm, 650-1000 rpm, 700-1000 rpm, 750-1000 rpm, 800-1000 rpm, 850-1000 rpm, 900-1000 rpm, 950-1000 rpm, 100-110 rpm, 100-120 rpm, 100-130 rpm, 100-140 rpm, 100-150 rpm, 100-160 rpm, 100-170 rpm, 100-180 rpm, 100-190 rpm, 100-200 rpm, 100-220 rpm, 100-240 rpm, 100-260 rpm, 100-280 rpm, 100-300 rpm, 100-325 rpm, 100-350 rpm, 100-375 rpm, 100-400 rpm, 100-425 rpm, 100-450 rpm, 100-475 rpm, 100-500 rpm, 100-550 rpm, 100-600 rpm, 100-650 rpm, 100-700 rpm, 100-750 rpm, 100-800 rpm, 100-850 rpm, 100-900 rpm, 100-950 rpm, 110-120 rpm, 120-130 rpm, 130-140 rpm, 140-150 rpm, 150-160 rpm, 160-170 rpm, 170-180 rpm, 180-190 rpm, 190-200 rpm, 200-220 rpm, 220-240 rpm, 240-260 rpm, 260-280 rpm, 280-300 rpm, 300-325 rpm, 325-350 rpm, 350-375 rpm, 375-400 rpm, 400-425 rpm, 425-450 rpm, 450-475 rpm, 475-500 rpm, 500-550 rpm, 550-600 rpm, 600-650 rpm, 650-700 rpm, 700-750 rpm, 750-800 rpm, 800-850 rpm, 850-900 rpm, 900-950 rpm, 100-200 rpm, 200-300 rpm, 300-400 rpm, 400-500 rpm, 500-600 rpm, 600-700 rpm, 700-800 rpm, 800-900 rpm, 900-1000 rpm, 150-250 rpm, 250-350 rpm, 350-450 rpm, 450-550 rpm, 550-650 rpm, 650-750 rpm, 750-850 rpm, or 850-950 rpm. In some embodiments, a stress-sensitive antibody that is sensitive to agitation is sensitive to spinning (e.g., rotating) at a speed in the range of 100-1000 rpm, 110- 1000 rpm, 120-1000 rpm, 130-1000 rpm, 140-1000 rpm, 150-1000 rpm, 160-1000 rpm, 170- 1000 rpm, 180-1000 rpm, 190-1000 rpm, 200-1000 rpm, 220-1000 rpm, 240-1000 rpm, 260- 1000 rpm, 280-1000 rpm, 300-1000 rpm, 325-1000 rpm, 350-1000 rpm, 375-1000 rpm, 400- 1000 rpm, 425-1000 rpm, 450-1000 rpm, 475-1000 rpm, 500-1000 rpm, 550-1000 rpm, 600- 1000 rpm, 650-1000 rpm, 700-1000 rpm, 750-1000 rpm, 800-1000 rpm, 850-1000 rpm, 900- 1000 rpm, 950-1000 rpm, 100-110 rpm, 100-120 rpm, 100-130 rpm, 100-140 rpm, 100-150 rpm, 100-160 rpm, 100-170 rpm, 100-180 rpm, 100-190 rpm, 100-200 rpm, 100-220 rpm, 100-240 rpm, 100-260 rpm, 100-280 rpm, 100-300 rpm, 100-325 rpm, 100-350 rpm, 100-375 rpm, 100-400 rpm, 100-425 rpm, 100-450 rpm, 100-475 rpm, 100-500 rpm, 100-550 rpm,28#14616800v2100-600 rpm, 100-650 rpm, 100-700 rpm, 100-750 rpm, 100-800 rpm, 100-850 rpm, 100-900 rpm, 100-950 rpm, 110-120 rpm, 120-130 rpm, 130-140 rpm, 140-150 rpm, 150-160 rpm, 160-170 rpm, 170-180 rpm, 180-190 rpm, 190-200 rpm, 200-220 rpm, 220-240 rpm, 240-260 rpm, 260-280 rpm, 280-300 rpm, 300-325 rpm, 325-350 rpm, 350-375 rpm, 375-400 rpm, 400-425 rpm, 425-450 rpm, 450-475 rpm, 475-500 rpm, 500-550 rpm, 550-600 rpm, 600-650 rpm, 650-700 rpm, 700-750 rpm, 750-800 rpm, 800-850 rpm, 850-900 rpm, 900-950 rpm, 100-200 rpm, 200-300 rpm, 300-400 rpm, 400-500 rpm, 500-600 rpm, 600-700 rpm, 700-800 rpm, 800-900 rpm, 900-1000 rpm, 150-250 rpm, 250-350 rpm, 350-450 rpm, 450-550 rpm, 550-650 rpm, 650-750 rpm, 750-850 rpm, or 850-950 rpm.

[0090] In some embodiments, a stress condition comprises exposure to an agitation stressor for a time period in the range of 1-24 hours, 2-24 hours, 3-24 hours, 4-24 hours, 5-24 hours, 6-24 hours, 7-24 hours, 8-24 hours, 9-24 hours, 10-24 hours, 11-24 hours, 12-24 hours, 13-24 hours, 14-24 hours, 15-24 hours, 16-24 hours, 17-24 hours, 18-24 hours, 19-24 hours, 20-24 hours, 21-24 hours, 22-24 hours, 23-24 hours, 1-2 hours, 1-3 hours, 1-4 hours, 1-5 hours, 1-6 hours, 1-7 hours, 1-8 hours, 1-9 hours, 1-10 hours, 1-11 hours, 1-12 hours, 1-13 hours, 1-14 hours, 1-15 hours, 1-16 hours, 1-17 hours, 1-18 hours, 1-19 hours, 1-20 hours, 1- 21 hours, 1-22 hours, 1-23 hours, 2-3 hours, 3-4 hours, 4-5 hours, 5-6 hours, 6-7 hours, 7-8 hours, 8-9 hours, 9-10 hours, 10-11 hours, 11-12 hours, 12-13 hours, 13-14 hours, 14-15 hours, 15-16 hours, 16-17 hours, 17-18 hours, 18-19 hours, 19-20 hours, 20-21 hours, 21-22 hours, 22-23 hours, 5-10 hours, 10-15 hours, 15-20 hours, 10-20 hours, 1-30 days, 2-30 days, 3-30 days, 4-30 days, 5-30 days, 6-30 days, 7-30 days, 8-30 days, 9-30 days, 10-30 days, 11- 30 days, 12-30 days, 13-30 days, 14-30 days, 15-30 days, 16-30 days, 17-30 days, 18-30 days, 19-30 days, 20-30 days, 22-30 days, 24-30 days, 26-30 days, 28-30 days, 1-2 days, 1-3 days, 1-4 days, 1-5 days, 1-6 days, 1-7 days, 1-8 days, 1-9 days, 1-10 days, 1-11 days, 1-12 days, 1-13 days, 1-14 days, 1-15 days, 1-16 days, 1-17 days, 1-18 days, 1-19 days, 1-20 days, 1-22 days, 1-24 days, 1-26 days, 1-28 days, 2-3 days, 3-4 days, 4-5 days, 5-6 days, 6-7 days, 7-8 days, 8-9 days, 9-10 days, 10-11 days, 11-12 days, 12-13 days, 13-14 days, 14-15 days, 15-16 days, 16-17 days, 17-18 days, 18-19 days, 19-20 days, 20-22 days, 22-24 days, 24-26 days, or 26-28 days.Multiple Stress Conditions

[0091] In some embodiments, a stress condition comprises one or more stressors. In some embodiments, a stress condition comprises a light stressor, a thermal stressor, and / or an agitation stressor. In some embodiments, a stress condition comprises a light stressor and a29#14616800v2thermal stressor. In some embodiments, a stress condition comprises a light stressor and an agitation stressor. In some embodiments, a stress condition comprises a thermal stressor and an agitation stressor. In some embodiments, a stress condition comprises a light stressor, a thermal stressor, and an agitation stressor.

[0092] In some embodiments, a stress condition comprises a first stressor and a second stressor. In some embodiments, the first stressor and the second stressor are different light stressors. In some embodiments, the first stressor and the second stressor are different thermal stressors. In some embodiments, the first stressor and the second stressor are different agitation stressors. In some embodiments, the first stressor is a light stressor and the second stressor is a thermal stressor. In some embodiments, the first stressor is a light stressor and the second stressor is an agitation stressor. In some embodiments, the first stressor is a thermal stressor and the second stressor is an agitation stressor. In some embodiments, the first stressor and the second stressor are independently selected from light stressors, thermal stressors, and agitation stressors. In some embodiments, the first stressor and second stressor occur simultaneously. In some embodiments, the first stressor and the second stressor occur in sequence (e.g., the second stressor occurs after the first stressor).

[0093] In some embodiments, a stress condition comprises exposure to two or more stressors (e.g., 2, 3, 4, or more stressors). In some embodiments, one or more of the two or more stressors is a light stressor. In some embodiments, one or more of the two or more stressors is a thermal stressor. In some embodiments, one or more of the two or more stressors is an agitation stressor. In some embodiments, the two or more stressors (e.g., 2, 3, 4, or more stressors) are each independently selected from light stressors, thermal stressors, and agitation stressors. In some embodiments, one or more of the two or more stressors occur simultaneously. In some embodiments, the two or more stressors occur simultaneously. In some embodiments, one or more of the two or more stressors occur in sequence (e.g., one of the two or more stressors occurs after another of the two or more stressors). In some embodiments, a stress condition comprises exposure to an agitation stressor and a thermal stressor. In some embodiments, a stress condition comprises exposure to an agitation stress at a temperature of 25-100°C, 26-100°C, 27-100°C, 28-100°C, 29-100°C, 30-100°C, 33.5- 100°C, 35-100°C, 37.5-100°C, 40-100°C, 42.5-100°C, 45-100°C, 47.5-100°C, 50-100°C, 55- 100°C, 60-100°C, 65-100°C, 70-100°C, 75-100°C, 80-100°C, 85-100°C, 90-100°C, 95- 100°C, 25-26°C, 25-27°C, 25-28°C, 25-29°C, 25-30°C, 25-32.5°C, 25-35°C, 25-37.5°C, 25- 40°C, 25-42.5°C, 25-45°C, 25-47.5°C, 25-50°C, 25-55°C, 25-60°C, 25-65°C, 25-70°C, 25- 75°C, 25-80°C, 25-85°C, 25-90°C, 25-95°C, 25-27°C, 27-28°C, 28-29°C, 29-30°C, SOSO#14616800v232.5°C, 32.5-35°C, 35-37.5°C, 37.5-40°C, 40-42.5°C, 42.5-45°C, 45-47.5°C, 47.5-50°C, 50- 55°C, 55-60°C, 60-65°C, 65-70°C, 70-75°C, 75-80°C, 85-90°C, 90-95°C, 25-35°C, 35-45°C, 45-55°C, 55-65°C, 65-75°C, 75-85°C, 85-95°C, 30-40°C, 40-50°C, 50-60°C, 60-70°C, 70- 80°C, 80-90°C, or 90-100°C. In some embodiments, a stress condition comprises exposure to 100-1000 rpm at a temperature of 25-100°C, e.g., 100-1000 rpm at a temperature of 25°C, 100-1000 rpm at a temperature of 30°C, 100-1000 rpm at a temperature of 40°C, 100-1000 rpm at a temperature of 50°C, 100-1000 rpm at a temperature of 60°C, 100-1000 rpm at a temperature of 70°C, 100-1000 rpm at a temperature of 80°C, 100-1000 rpm at a temperature of 90°C, or 100-1000 rpm at a temperature of 100°C. In some embodiments, a stress condition comprises exposure to 100-1000 rpm at a temperature of 25-100°C for at least 1 day, e.g., at least 2 days, at least 3 days, or more. In some embodiments, a stress condition comprises exposure to 100-1000 rpm at a temperature of 25-100°C for at least 3 days, e.g., 100-1000 rpm at a temperature of 25°C for at least 3 days, 100-1000 rpm at a temperature of 30°C for at least 3 days, 100-1000 rpm at a temperature of 40°C for at least 3 days, 100-1000 rpm at a temperature of 50°C for at least 3 days, 100-1000 rpm at a temperature of 60°C for at least 3 days, 100-1000 rpm at a temperature of 70°C for at least 3 days, 100-1000 rpm at a temperature of 80°C for at least 3 days, 100-1000 rpm at a temperature of 90°C for at least 3 days, or 100-1000 rpm at a temperature of 100°C for at least 3 days.Illustrative Effects of Stress Conditions

[0094] In some embodiments, a stress-sensitive antibody undergoes a structural change (e.g., physical change, chemical change) when subjected to one or more stress conditions described herein relative to an antibody that is not stress-sensitive. For example, a lightsensitive, temperature-sensitive, and / or agitation-sensitive antibody may undergo a structural change (e.g., degradation, aggregation, oxidation, di-oxidation, post-translational modification (PTM)) when subjected to one or more light, thermal, and / or agitation stress conditions comprises herein relative to antibody that is not sensitive to the stressor.

[0095] In some embodiments, formulating a stress-sensitive antibody in a composition described herein promotes resistance of the antibody to the stress conditions. For example, formulating a light-sensitive, temperature-sensitive, and / or agitation-sensitive antibody in a composition described herein may promote resistance of the antibody to a light, thermal, and / or agitation stressor, respectively.31#14616800v2Physical Changes

[0096] In some embodiments, a stress-sensitive antibody undergoes one or more physical changes when subjected to one or more stress conditions described herein relative to an antibody that is not stress-sensitive. In some embodiments, the physical change comprises degradation. In some embodiments, the physical change comprises aggregation of the antibody.Degradation

[0097] In some embodiments, a stress-sensitive antibody is degraded when subjected to one or more stress conditions described herein relative to an antibody that is not stresssensitive. In some embodiments, formulating a stress-sensitive antibody in a composition described here promotes resistance of the antibody to the stress conditions by reducing degradation of the antibody. In some embodiments, an antibody is said to “be degraded” or “be degrading” when degradation products having molecular weights lower than that of the antibody are formed in the composition (“low molecular weight degradation products”). As used herein, “low molecular weight degradation products” or “low molecular weight impurities”, used synonymously herein, refer to fragments of an antibody (e.g., molecules or peptides that are of a lower molecular weight of the antibody) that are generated when the antibody undergoes a degradation process. Degradation may be measured using any method known in the art. In some embodiments, measuring degradation comprises measuring the amount (e.g., absolute amount, relative amount) of low molecular weight products in a composition comprising stress-sensitive antibodies; for example, the amount may comprise a ratio (e.g., percentage) of low molecular weight products relative to native antibody products. In some embodiments, a low molecular weight degradation product is separated from the native antibody (e.g., for determining amount of the low molecular weight degradation product in a composition) by size-exclusion chromatography, reduced capillary electrophoresis-sodium dodecyl sulfate (CE-SDS), and / or non-reduced CE-SDS.

[0098] Aggregation

[0099] In some embodiments, a stress-sensitive antibody aggregates when subjected to one or more stress conditions described herein relative to an antibody that is not stresssensitive. In some embodiments, formulating a stress-sensitive antibody in a composition described here promotes resistance of the antibody to the stress conditions by reducing aggregation of the antibody. Protein aggregation can occur when proteins unfold or misfold due to various factors such as heat, pH changes, oxidative stress, mutations, or any of the32#14616800v2stresses described herein. Unfolded or misfolded proteins may then interact with each other and aggregate into insoluble complexes. In some embodiments, an aggregate is a covalent aggregate. In some embodiments, an aggregate is a non-covalent aggregate. In some embodiments, an antibody is said to “be aggregated” or “be aggregating” when aggregation products having molecular weights higher than that of the antibody are formed in the composition (“high molecular weight aggregates”). As used herein, “high molecular weight aggregates” refer to accumulations of antibodies or fragments thereof that are generated when the antibody undergoes an aggregation process. Aggregation may be measured using any method known in the art. In some embodiments, measuring aggregation comprises measuring the amount (e.g., absolute amount, relative amount) of high molecular weight products in a composition comprising stress-sensitive antibodies; for example, the amount may comprise a ratio (e.g., percentage) of high molecular weight aggregates relative to native antibody. In some embodiments, a high molecular weight aggregate is separated from the native antibody (e.g., for determining amount of the high molecular weight aggregate in a composition) by size-exclusion chromatography, reduced capillary electrophoresis-sodium dodecyl sulfate (CE-SDS), and / or non-reduced CE-SDS.[000100]Chemical Changes[000101] In some embodiments, a stress-sensitive antibody becomes chemically unstable when subjected to one or more stress conditions described herein. In some embodiments, an antibody is chemically unstable if it forms a charged variant. As used herein, a charged variant of an antibody refers to a form of the antibody that differs from the typical or reference form in terms of its overall net charge. In some embodiments, an antibody is chemically unstable if it forms cleavage products. As used herein, an antibody cleavage product refers to a fragment of an antibody that has been generated through the cleavage of peptide bonds within the antibody sequence. In some embodiments, a cleavage product is produced by chemical cleavage. In some embodiments, a cleavage product is produced by mechanical disruption (e.g., agitation).Oxidation and Di-oxidation[000102] In some embodiments, a stress-sensitive antibody is oxidized when subjected to one or more stress conditions described herein. As used herein, “oxidation” of an antibody refers to a chemical process in which an antibody undergoes oxidative reactions, resulting in the addition of oxygen atoms or oxygen-containing functional groups to the antibody. In some embodiments, oxidation occurs as a result of exposure to light. In some embodiments, 33#14616800v2oxidation occurs as a result of exposure to reactive oxygen species (ROS) or other oxidative agents, such as free radicals, hydrogen peroxide, or certain metal ions. In some embodiments, cysteine, methionine, tryptophan, tyrosine, and / or histidine residues are particularly susceptible to oxidation. In some embodiments, a cysteine residue is oxidized to form disulfide bonds or sulfenic acid (-SOH). In some embodiments, a methionine residue is oxidized to form methionine sulfoxide (-SO2H). In some embodiments, a tyrosine residue is oxidized to form a tyrosine radical or o,o'-dityrosine crosslinks. In some embodiments, a tryptophan is oxidized, followed by the loss of a -C6H5N group (tryptophan-C6H5N). In some embodiments, a histidine is oxidized, followed by the loss of a HCN group (histidine- HCN). In some embodiments, oxidation of a stress-sensitive antibody is measured via mass spectrometry (e.g., LC-MS / MS). For example, a tryptophan that undergoes a tryptophan- C6H5N di-oxidation modification may show a theoretical mass change of -59.052 Da as measured by LC-MS / MS, due to the addition of a di-oxygen molecule and the loss of a - C6H5N group. Likewise, a histidine that undergoes a histidine-HCN di-oxidation may show a theoretical mass change of 4.9789 Da as measured by LC-MS / MS, due to the addition of a dioxygen molecule and the loss of a -HCN group. See Zhang et al., J Pharm Sci. 2022 Jun; 111(6): 1556-1564, the entirety of which is incorporated by reference herein, for nonlimiting examples of amino acid oxidative modifications that may occur when a stresssensitive antibody described herein is subjected to stress (e.g., light, agitation, and / or thermal stress).[000103] In some embodiments, a stress-sensitive antibody is di-oxidized when subjected to one or more stress conditions described herein. As used herein, “di-oxidation” refers to a situation wherein an antibody undergoes oxidation at two distinct sites. In some embodiments, when di-oxidation of an antibody occurs, two separate oxidative modifications occur within the same antibody, resulting in the addition of oxygen atoms or oxygencontaining functional groups to two different locations. In some embodiments, a stresssensitive antibody is tri-oxidized when subjected to one or more stress conditions described herein. As used herein, “tri -oxidation” refers to a situation wherein an antibody undergoes oxidation at three distinct sites. In some embodiments, when tri-oxidation of an antibody occurs, three separate oxidative modifications occur within the same antibody, resulting in the addition of oxygen atoms or oxygen-containing functional groups to three different locations.34#14616800v2Post-Translational Modifications[000104] In some embodiments, stress-sensitive antibodies comprise amino acid residues susceptible to one or more post-translational modifications (PTMs) (e.g., pyro-glutamic acid formation, isomerization, glycation, deamidation, or succinimide formation). As referred to herein, an amino acid residue is “susceptible” to a PTM if said amino acid is able to be undergo one or more PTMs. In some embodiments, stress-sensitive antibodies undergo PTMs when subjected to light and / or thermal stress conditions. In some embodiments, a PTM affects an antibody’s stability, activity, and / or interactions with other molecules.[000105] In some embodiments, a stress-sensitive antibody is susceptible to the formation of a pyro-glutamic acid (i.e., pyro-glutamate or 5-oxoproline) on an N-terminal glutamine residue of the antibody. Pyro-glutamic acid is formed when an N-terminal glutamine residue of an antibody undergoes cyclization, resulting in the loss of ammonia and water. This cyclization process leads to the formation of a cyclic structure with a terminal pyro-glutamic acid residue.[000106] In some embodiments, a stress-sensitive antibody is susceptible to isomerization. As used herein, “isomerization” refers to the conversion of one structural isomer of an antibody into another. In some embodiments, isomerization involves rearrangement of the atoms within the antibody, resulting in a change in its three-dimensional structure. In some embodiments, isomerization comprises a conversion between the cis and trans configurations of peptide bonds.[000107] In some embodiments, a stress-sensitive antibody is susceptible to glycation.Generally, glycation involves the non-enzymatic addition of a sugar molecule to an antibody, forming a covalent bond between the sugar and an amino acid within the protein structure. In some embodiments, an antibody is glycated with glucose. In some embodiments, glycation occurs to one or more lysine and / or arginine residues of an antibody.[000108] In some embodiments, a stress-sensitive antibody is susceptible to deamidation. Generally, deamidation involves the conversion of an amino acid residue (e.g., asparagine (N) to aspartic acid (D) or glutamine (Q) to glutamic acid (E)) through the hydrolysis of an amide side chain.[000109] In some embodiments, a PTM is succinimide formation. Generally, succinimide formation involves the cyclization of asparagine (Asn) residues, resulting in the transient formation of a succinimide intermediate. The succinimide intermediate can undergo further reactions, such as hydrolysis or racemization, leading to the conversion of asparagine residues to either aspartic acid or isoaspartic acid residues.35#14616800v2[000110] In some embodiments, identity, presence and / or an amount of PTMs in a stresssensitive antibody is measured via any method known in the art, such as peptide mapping. Non-limiting examples of methods of identifying and / or determining presence and / or amount of PTMs are described by Witze, Eric S., et al. "Mapping protein post-translational modifications with mass spectrometry." Nature methods 4.10 (2007): 798-806; and Shumyantseva, Victoria V., et al. "Electrochemical methods for detection of post- translational modifications of proteins." Biosensors and Bioelectronics 61 (2014): 131-139.Methods for Assessing Composition Stability[000111] As used herein, the “physical stability of a formulation” refers to properties of a formulation that indicate stability over time. In some embodiments, these properties are color, appearance, pH, turbidity, and protein concentration. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein exhibit increased physical stability relative to compositions comprising the same stress-sensitive antibodies formulated differently.[000112] In some embodiments, a solution is said to be physically stable via assessment by visible inspection if it is clear-to-slightly opalescent, essentially free of visible particulates (i.e., is not turbid), and / or colorless-to-pale yellow as compared to a standard control.[000113] In some embodiments, the turbidity of a solution is caused by formation of visible particles. In some embodiments, the presence of visible particles in solution is detected by visual inspection. In some embodiments, particular matter analysis is performed by light obscuration (HIAC), which can measure subvisible particles that are > 2 pm in size.[000114] In some embodiments, antibody stability is assessed through the formation of sub- visible particles. As used herein, sub-visible particles refer to particles or aggregates that form in a composition that are too small to be detected by standard visible inspection techniques. In some embodiments, a sub-visible particle has a size in the range of 0.1-10 pm, 0.2-10 pm, 0.3-10 pm, 0.4-10 pm, 0.5-10 pm, 0.6-10 pm, 0.7-10 pm, 0.8-10 pm, 0.9-10 pm, 1-10 pm, 1.1-10 pm, 1.2-10 pm, 1.3-10 pm, 1.4-10 pm, 1.5-10 pm, 1.7-10 pm, 1.8-10 pm, 1.9-10 pm, 2-10 pm, 2.2-10 pm, 2.4-10 pm, 2.6-10 pm, 2.8-10 pm, 3-10 pm, 3.25-10 pm, 3.5-10 pm, 3.75-10 pm, 4-10 pm, 4.25-10 pm, 4.5-10 pm, 4.75-10 pm, 5-10 pm, 5.5-10 pm, 6-10 pm, 6.5-10 pm, 7-10 pm, 7.5-10 pm, 8-10 pm, 8.5-10 pm, 9-10 pm, 9.5-10 pm, 0.1-0.2 pm, 0.1-0.3 pm, 0.1-0.4 pm, 0.1-0.5 pm, 0.1-0.6 pm, 0.1-0.7 pm, 0.1-0.8 pm, 0.1-0.9 pm, 0.1-1 pm, 0.1-1.1 pm, 0.1-1.2 pm, 0.1-1.3 pm, 0.1-1.4 pm, 0.1-1.5 pm, 0.1-1.6 pm, 0.1-1.7 pm, 0.1-1.8 pm, 0.1-1.9 pm, 0.1-2 pm, 0.1-2.2 pm, 0.1-2.4 pm, 0.1-2.6 pm, 0.1-2.8 pm, 0.1-36#14616800v23 pm, 0.1-3.25 pm, 0.1-3.5 pm, 0.1-3.75 pm, 0.1-4 pm, 0.1-4.25 pm, 0.1-4.5 pm, 0.1-4.75 pm, 0.1-5 pm, 0.1-5.5 pm, 0.1-6 pm, 0.1-6.5 pm, 0.1-7 pm, 0.1-7.5 pm, 0.1-8 pm, 0.1-8.5 pm, 0.1-9 pm, 0.1-9.5 pm, 0.2-0.3 pm, 0.3-0.4 pm, 0.4-0.5 pm, 0.5-0.6 pm, 0.6-0.7 pm, 0.7- 0.8 pm, 0.8-0.9 pm, 0.9-1 pm, 1-1.1 pm, 1.1-1.2 pm, 1.2-1.3 pm, 1.3-1.4 pm, 1.4-1.5 pm,1.5-1.6 pm, 1.6-1.7 pm, 1.7-1.8 pm, 1.8-1.9 pm, 1.9-2 pm, 2-2.2 pm, 2.2-2.4 pm, 2.4-2.6 pm, 2.6-2.8 pm, 2.8-3 pm, 3-3.25 pm, 3.25-3.5 pm, 3.5-3.75 pm, 3.75-4 pm, 4-4.25 pm, 4.25-4.5 pm, 4.5-4.75 pm, 4.75-5 pm, 5-5.5 pm, 5.5-6 pm, 6-6.5 pm, 6.5-7 pm, 7-7.5 pm,7.5-8 pm, 8-8.5 pm, 8.5-9 pm, or 9-9.5 pm.[000115] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein preserve antibody concentration (e.g., reduce loss of antibody concentration) relative to compositions comprising the same stress-sensitive antibodies formulated differently. In some embodiments, antibody concentration is measured by UV absorbance, using the extinction coefficient and Beer’s Law (e.g., The Beer-Lambert Law). In some embodiments, determining a reduction in antibody concentration comprises determining the difference in antibody concentration (e.g., using UV absorbance) at a first time point and at a second later time point.[000116] As used herein, “chemical instability of a formulation” refers to the formation of covalently modified forms (e.g., aggregates, degradation (e.g., cleavage) products, charged variant forms) and non-covalently modified forms (e.g., non-covalent aggregates) of antibodies within a formulation. As such “chemical stability of a formulation” refers to the resistance of antibodies in a formulation to the formation of covalently and non-covalently modified forms. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein exhibit increased chemical stability relative to compositions comprising the same stress-sensitive antibodies formulated differently.[000117] In some embodiments, a composition is said to be chemically stable via assessment of high molecular weight aggregates and low molecular weight degradation products in the composition. In some embodiments, high molecular weight aggregates and low molecular weight degradation products are assessed via separation from a native antibody by sizeexclusion chromatography (SEC) (e.g., size exclusion high performance liquid chromatography (SE-HPLC)). In some embodiments, high molecular weight aggregates and low molecular weight degradation products are assessed via separation from a native antibody by reduced and / or non-reduced capillary electrophoresis sodium dodecyl sulfate (CE-SDS) methods. In some embodiments, the percentage of degraded material (e.g., low37#14616800v2molecular weight degradation products) is calculated from the ratio of the area of non-native peaks to the total antibody -related peaks (e.g., as calculated from chromatograph results).[000118] In some embodiments, a composition is said to be chemically stable via assessment of charged protein variants in the composition. In some embodiments, charged protein variants in a composition are assessed using cation exchange chromatography (CEX). In some embodiments, chromatography peaks with retention times earlier than that of the main peak (e.g., a peak for a native antibody) are labeled as “acidic” peaks. In some embodiments, chromatography peaks with retention times later than that of the main peak (e.g., a peak for a native protein) are labeled as “basic” peaks.Illustrative Formulations[000119] In some aspects, the present disclosure relates to compositions comprising a stresssensitive antibody formulated with histidine, and optionally methionine, in amounts effective to promote resistance of the antibody to one or more stress conditions described herein. In some embodiments, the compositions described herein promote resistance of the antibody to a light, thermal, and / or agitation stressor. In some embodiments, the compositions described herein improve the appearance of the composition relative to control compositions (e.g., under stress conditions).[000120] Concentrations (e.g., of components of a formulation provided herein) may be expressed using various units, e.g., w / v, %w / v, molar ratio, mM). One of skill in the art will understand that concentrations may be provided according to a first unit or mode of expression and be equivalent to second unit or mode of expression. For example, a concentration expressed as mg / mL can be expressed as mM. Conversions between units and modes of expression of concentration are known in the art; certain examples of conversions are provided herein.[000121] In some embodiments, a concentration of a component in a solution is provided in a ratio of weight (w) by volume (v), e.g., using units for weight (e.g., milligrams (mg), grams (g), kilograms (kg)) or volume (e.g., milliliter (mL), liters (L), kiloliters (kL)); for example, the concentration of a component in a solution may be provided as a ratio of the mass of the component (w) per unit of the solution (v) (“w / v”), e.g., mg / mL.[000122] In some embodiments, a concentration of a component in a solution is provided as a percentage of the total mass of the component in grams (W) by the total volume of the38#14616800v2solution in milliliters (V) (“w / v”), i.e., “% w / v”. % w / v of a particular component of a solution may be calculated according to the following formula: 100wherein p is % w / v of a component in a solution; W is the total mass of the component in the solution in g; and Lis the total volume of the solution in mL.[000123] In some embodiments, a concentration is provided as a molar ratio. A molar ratio represents the total number of moles of a first substance to the total number of moles of a second substance in a composition (e.g., in a solution); for example, a solution containing a 3 moles of substance A to every 1 mole of substance B may be expressed as “3: 1 A:B”. The number of moles of a particular component in a solution can be calculated according to the following formula: w n = — M wherein n is the number of moles of the component in the solution; w is the mass of the component in the solution; and AT is the weight of one mole of the component.[000124] In some embodiments, a concentration is provided in millimolar (mM) units; millimolar units represent the total number of millimoles of a component of a solution in 1 liter of solution. A millimolar concentration of a particular component can be calculated from a weight / volume ratio according to the following formula: 1000wherein mM is the millimolar concentration; w is the mass of the component in the solution; v is the total volume of a solution containing the component; and AT is the weight of one mole of the component.[000125] In some embodiments, a composition comprises a stress-sensitive antibody at a concentration of at least 120 mg / mL, at least 130 mg / mL, at least 140 mg / mL, at least 150 mg / mL, at least 160 mg / mL, at least 170 mg / mL, at least 180 mg / mL, at least 190 mg / mL, at least 200 mg / mL, at least 220 mg / mL, at least 240 mg / mL, at least 260 mg / mL, at least 280 mg / mL, at least 300 mg / mL, at least 325 mg / mL, at least 350 mg / mL, at least 375 mg / mL, at least 400 mg / mL, at least 425 mg / mL, at least 450 mg / mL, at least 475 mg / mL, or at least 500 mg / mL. In some embodiments, a composition comprises a stress-sensitive antibody at a concentration in the range of 120-500 mg / mL, 130-500 mg / mL, 140-500 mg / mL, 150-500 mg / mL, 160-500 mg / mL, 170-500 mg / mL, 180-500 mg / mL, 190-500 mg / mL, 200-500 mg / mL, 220-500 mg / mL, 240-500 mg / mL, 260-500 mg / mL, 280-500 mg / mL, 300-50039#14616800v2mg / mL, 325-500 mg / mL, 350-500 mg / mL, 375-500 mg / mL, 400-500 mg / mL, 425-500 mg / mL, 450-500 mg / mL, 475-500 mg / mL, 120-130 mg / mL, 120-140 mg / mL, 120-150 mg / mL, 120-160 mg / mL, 120-170 mg / mL, 120-180 mg / mL, 120-190 mg / mL, 120-200 mg / mL, 120-220 mg / mL, 120-240 mg / mL, 120-260 mg / mL, 120-280 mg / mL 120-300 mg / mL, 120-325 mg / mL, 120-350 mg / mL, 120-375 mg / mL, 120-400 mg / mL, 120-425 mg / mL, 120-450 mg / mL, 120-475 mg / mL, 130-140 mg / mL, 140-150 mg / mL, 150-160 mg / mL, 160-170 mg / mL, 170-180 mg / mL, 180-190 mg / mL, 190-200 mg / mL, 200-220 mg / mL, 220-240 mg / mL, 240-260 mg / mL, 260-280 mg / mL, 280-300 mg / mL, 300-325 mg / mL, 325-350 mg / mL, 350-375 mg / mL, 375-400 mg / mL, 400-425 mg / mL, 425-450 mg / mL, or 450-475 mg / mL. In some embodiments, a composition comprises a stresssensitive antibody at a concentration in the range of 150-175 mg / mL, 155-175 mg / mL, 160- 175 mg / mL, 165-175 mg / mL, 170-175 mg / mL, 150-155 mg / mL, 150-160 mg / mL, 150-165 mg / mL, 150-170 mg / mL, 155-160 mg / mL, 160-165 mg / mL, or 165-170 mg / mL. In some embodiments, a composition comprises a stress-sensitive antibody at a concentration of 175 mg / mL. In some embodiments, a composition comprises a stress-sensitive antibody at a concentration of 150 mg / mL.[000126] In some embodiments, the composition comprises histidine (e.g., a histidine buffer) in amount effective to promote resistance of the antibody to stress (e.g., thermal, agitation, and / or light stress). In some embodiments, the molar ratio of histidine to the antibody in the composition is in the range of 12:1-160:1, 13:1-160:1, 14:1-160:1, 15:1- 160:1, 16:1-160:1, 17:1-160:1, 18:1-160:1, 19:1-160:1,20:1-160:1,22:1-160:1,24:1-160:1, 26:1-160:1, 28:1-160:1, 30:1-160:1, 32.5:1-160:1, 35:1-160:1, 37.5:1-160:1, 40:1-160:1, 42.5:1-160:1, 45:1-160:1, 47.5:1-160:1, 50:1-160:1, 55:1-160:1, 60:1-160:1, 65:1-160:1, 70:1-160:1, 75:1-160:1, 80:1-160:1, 85:1-160:1, 90:1-160:1, 95:1-160:1, 100:1-160:1, 110:1- 160:1, 120:1-160:1, 130:1-160:1, 140:1-160:1, 150:1-160:1, 12:1-13:1, 12:1-14:1, 12:1-15:1, 12:1-16:1, 12:1-17:1, 12:1-18:1, 12:1-19:1, 12:1-20:1, 12:1-22:1, 12:1-24:1, 12:1-26:1, 12:1- 28:1, 12:1-30:1, 12:1-32.5:1, 12:1-35:1, 12:1-37.5:1, 12:1-40:1, 12:1-42.5:1, 12:1-45:1, 12:1- 47.5:1, 12:1-50:1, 12:1-55:1, 12:1-60:1, 12:1-65:1, 12:1-70:1, 12:1-75:1, 12:1-80:1, 12:1- 85:1, 12:1-90:1, 12:1-95:1, 12:1-100:1, 12:1-110:1, 12:1-120:1, 12:1-130:1, 12:1-140:1, 12:1- 150:1, 13:1-14:1, 14:1-15:1, 15:1-16:1, 16:1-17:1, 17:1-18:1, 18:1-19:1, 19:1-20:1,20:1- 22:1, 22:1-24:1, 24:1-26:1, 26:1-28:1, 28:1-30:1, 30:1-32.5:1, 32.5:1-35:1, 35:1-37.5:1, 37.5:1-40:1, 40:1-42.5:1, 42.5:1-45:1, 45:1-47.5:1, 47.5:1-50:1, 50:1-55:1, 55:1-60:1, 60:1- 65:1, 65:1-70:1, 70:1-75:1, 75:1-80:1, 80:1-85:1, 85:1-90:1, 90:1-95:1, 95:1-100:1, 100:1- 110:1, 110:1-120:1, 120:1-130:1, 130:1-140:1, or 140:1-150. In some embodiments, the40#14616800v2composition comprises histidine at a concentration in the range of 20-150mM, 22-150 mM, 24-150 mM, 26-150 mM, 28-150 mM, 30-150 mM, 32.5-150 mM, 35-150 mM, 37.5-150 mM, 40-150 mM, 42.5-150 mM, 45-150 mM, 47.5-150 mM, 50-150 mM, 55-150 mM, 60- 150 mM, 65-150 mM, 70-150 mM, 75-150 mM, 80-150 mM, 85-150 mM, 90-150 mM, 95- 150 mM, 100-150 mM, 110-150 mM, 120-150 mM, 130-150 mM, 140-150 mM, 20-100 mM, 22-100 mM, 24-100 mM, 26-100 mM, 28-100 mM, 30-100 mM, 32.5-100 mM, 35-100 mM, 37.5-100 mM, 40-100 mM, 42.5-100 mM, 45-100 mM, 47.5-100 mM, 50-100 mM, 55- 100 mM, 60-100 mM, 65-100 mM, 70-100 mM, 75-100 mM, 80-100 mM, 85-100 mM, 90- 100 mM, 95-100 mM, 20-22 mM, 20-24 mM, 20-26 mM, 20-28 mM, 20-30 mM, 20-32.5 mM, 20-35 mM, 20-37.5 mM, 20-40 mM, 20-42.5 mM, 20-45 mM, 20-47.5 mM, 20-50 mM, 20-55 mM, 20-60 mM, 20-65 mM, 20-70 mM, 20-75 mM, 20-80 mM, 20-85 mM, 20-90 mM, 20-95 mM, 22-24 mM, 24-26 mM, 26-28 mM, 28-30 mM, 30-32.5 mM, 32.5-35 mM, 35-37.5 mM, 37.5-40 mM, 40-42.5 mM, 42.5-45 mM, 45-47.5 mM, 47.5-50 mM, 50-55 mM, 55-60 mM, 60-65 mM, 65-70 mM, 70-75 mM, 75-80 mM, 80-85 mM, 85-90 mM, or 90-95 mM. In some embodiments, the composition comprises histidine at a concentration of 100 mM. In some embodiments, the composition comprises histidine at a concentration of 50 mM. In some embodiments, the histidine is L-histidine. In some embodiments, the histidine is D-histidine. In some embodiments, the histidine is protonated (H+-His) (e.g., at a physiological pH). In some embodiments, the histidine is deprotonated. In some embodiments, the histidine is a histidine salt. In some embodiments, the histidine salt is histidine monohydrochloride (His-HCl; e.g., L-histidine monohydrochloride (L-His-Hcl)), histidine dihydrochloride (His-2HC1), histidine sulfate (His-H2SO4), histidine acetate (His- CH3COOH), histidine citrate (His-C6H8O7), or histidine phosphate (His-H3PO4). In some embodiments, the histidine is N(alpha)-acetyl histidine (NAH). In some embodiments, the histidine is 1-methyl-histidine or 3-methyl histidine. In some embodiments, the composition comprises L-histidine. In some embodiments, the composition comprises His-HCl (e.g., L- His-Hcl).[000127] In some embodiments, the composition further comprises methionine (e.g., a methionine buffer) in amount effective to promote resistance of the antibody to stress (e.g., thermal, agitation, and / or light stress). In some embodiments, the molar ratio of methionine to the antibody in the composition is in the range of 0: 1-20: 1, 1: 1-20: 1, 2: 1-20: 1, 3: 1-20: 1, 4: 1- 20: 1, 5: 1-20: 1, 6: 1-20: 1, 7: 1-20: 1, 8: 1-20: 1, 9: 1-20: 1, 10: 1-20: 1, 11 : 1-20: 1, 12: 1-20: 1, 13: 1- 20: 1, 14: 1-20: 1, 15: 1-20: 1, 16: 1-20: 1, 17: 1-20: 1, 18: 1-20: 1, 19: 1-20: 1, 0: 1-1 : 1, 0: 1-2: 1, 0: 1- 3: 1, 0: 1-4: 1, 0: 1-5: 1, 0: 1-6: 1, 0: 1-7: 1, 0: 1-8: 1, 0: 1-9: 1, 0: 1-10: 1, 0: 1-11 : 1, 0: 1-12: 1, 0: 1-13: 1, 41#14616800v20: 1-14: 1, 0: 1-15: 1, 0: 1-16: 1, 0: 1-17: 1, 0: 1-18: 1, 0: 1-19: 1, 1 :l-2: 1, 2: 1-3: 1, 3: 1-4: 1, 4: 1-5: 1, 5:1-6: 1, 6:1-7: 1, 7: 1-8: 1, 8:1-9: 1, 9: 1-10: 1, 10: 1-11 : 1, 11 : 1-12: 1, 12: 1-13: 1, 13: 1-14: 1, 14: 1- 15: 1, 15: 1-16: 1, 16: 1-17: 1, 17: 1-18: 1, 18: 1-19: 1, 0: 1-5: 1, 5: 1-10: 1, 10: 1-15: 1, or 15: 1-20. In some embodiments, the composition comprises methionine at a concentration in the range of 0-20 mM, 1-20 mM, 2-20 mM, 3-20 mM, 4-20 mM, 5-20 mM, 6-20 mM, 7-20 mM, 8-20 mM, 9-20 mM, 10-20 mM, 11-20 mM, 12-20 mM, 13-20 mM, 14-20 mM, 15-20 mM, 16-20 mM, 17-20 mM, 18-20 mM, 19-20 mM, 0-1 mM, 0-2 mM, 0-3 mM, 0-4 mM, 0-5 mM, 0-6 mM, 0-7 mM, 0-8 mM, 0-9 mM, 0-10 mM, 0-11 mM, 0-12 mM, 0-13 mM, 0-14 mM, 0-15 mM, 0-16 mM, 0-17 mM, 0-18 mM, 0-19 mM, 1-2 mM, 2-3 mM, 3-4 mM, 4-5 mM, 5-6 mM, 6-7 mM, 7-8 mM, 8-9 mM, 9-10 mM, 10-11 mM, 11-12 mM, 12-13 mM, 13-14 mM,14-15 mM, 15-16 mM, 16-17 mM, 17-18 mM, 18-19 mM, 0-5 mM, 5-10 mM, 10-15 mM, or15-20 mM. In some embodiments, the composition comprises methionine at a concentration of 10 mM. In some embodiments, the methionine is D-methionine. In some embodiments, the methionine is L-methionine. In some embodiments, the methionine is a methionine salt. In some embodiments, the methionine salt is methionine monohydrochloride (Met-HCl; e.g., L- methionine monohydrochloride (L-Met-Hcl)), methionine dihydrochloride (Met-2HC1), methionine sulfate (Met-H2SO4), methionine acetate (Met-CH3COOH), methionine citrate (Met-C6H8O7), or methionine phosphate (Met-H3PO4). In some embodiments, the methionine is methionine sulfoxide. In some embodiments, the methionine is N-Acetyl- Methionine. In some embodiments, the composition comprises L-methionine. In some embodiments, the composition comprises Met-HCl (e.g., L-Met-Hcl).[000128] In some embodiments, the composition further comprises arginine (e.g., an arginine buffer). In some embodiments, the composition comprises arginine at a concentration in the range of 10-500 mM, 20-500 mM, 30-500 mM, 40-500 mM, 50-500 mM, 60-500 mM, 70-500 mM, 80-500 mM, 90-500 mM, 100-500 mM, 150-500 mM, 200- 500 mM, 250-500 mM, 300-500 mM, 350-500 mM, 400-500 mM, 450-500 mM, 10-400 mM, 20-400 mM, 30-400 mM, 40-400 mM, 50-400 mM, 60-400 mM, 70-400 mM, 80-400 mM, 90-400 mM, 100-400 mM, 150-400 mM, 200-400 mM, 250-400 mM, 300-400 mM, 350-400 mM, 10-300 mM, 20-300 mM, 30-300 mM, 40-300 mM, 50-300 mM, 60-300 mM, 70-300 mM, 80-300 mM, 90-300 mM, 100-300 mM, 150-300 mM, 200-300 mM, 250-300 mM, 300-300 mM, 350-300 mM, 10-250 mM, 20-250 mM, 30-250 mM, 40-250 mM, 50-250 mM, 60-250 mM, 70-250 mM, 80-250 mM, 90-250 mM, 100-250 mM, 150-250 mM, 200- 250 mM, 10-200 mM, 20-200 mM, 30-200 mM, 40-200 mM, 50-200 mM, 60-200 mM, 70- 200 mM, 80-200 mM, 90-200 mM, 100-200 mM, 110-200 mM, 120-200 mM, 130-200 mM, 42#14616800v2140-200 mM, 150-200 mM, 160-200 mM, 170-200 mM, 180-200 mM, 190-200 mM, 50-150 mM, 55-150 mM, 60-150 mM, 65-150 mM, 70-150 mM, 75-150 mM, 80-150 mM, 85-150 mM, 90-150 mM, 95-150 mM, 100-150 mM, 110-150 mM, 120-150 mM, 130-150 mM, 140- 150 mM, 50-55 mM, 50-60 mM, 50-65 mM, 50-70 mM, 50-75 mM, 50-80 mM, 50-85 mM, 50-90 mM, 50-95 mM, 50-100 mM, 50-110 mM, 50-120 mM, 50-130 mM, 50-140 mM, 55- 60 mM, 60-65 mM, 65-70 mM, 70-75 mM, 75-80 mM, 80-85 mM, 85-90 mm, 90-95 mM, 95-100 mM, 100-110 mM, 110-120 mM, 120-130 mM, or 130-140 mM. In some embodiments, the arginine is L-arginine. In some embodiments, the arginine is D-arginine. In some embodiments, the arginine is arginine salt. In some embodiments, the arginine salt is arginine monohydrochloride (Arg-HCl; e.g., L-arginine monohydrochloride (L-Arg-HCl)), arginine dihydrochloride (Arg-2HC1), arginine sulfate (Arg-H2SO4), arginine acetate (Arg- CH3COOH), arginine citrate (Arg-C6H8O7), or arginine phosphate (Arg-H3PO4). In some embodiments, the arginine is dimethyl-arginine. In some embodiments, the composition comprises Arg-HCl (e.g., L-Arg-Hcl).[000129] In some embodiments, the composition has a pH of 5.3-5.9, 5.4-5.9, 5.5-5.9, 5.6- 5.9, 5.7-5.9, 5.8-5.9, 5.3-5.4, 5.3-5.5, 5.3-5.6, 5.3-5.7, 5.3-5.8, 5.4-5.5, 5.5-5.6, 5.6-5.7, or 5.7-5.8. In some embodiments, the composition has a pH of at least 5.3, at least 5.4, at least 5.5, at least 5.6, at least 5.7, at least 5.8, or at least 5.9. In some embodiments, the composition has a pH of 5.6.[000130] In some embodiments, the composition further comprises a surfactant. In some embodiments, a surfactant is polysorbate. In some embodiments, polysorbate is polysorbate 80, polysorbate 20, polysorbate 60, or polysorbate 40. In some embodiments, a surfactant is sodium dodecyl sulfate (SDS) (also known as sodium lauryl sulfate (SLS), sodium laureth sulfate (SLES; also known as sodium lauryl ether sulfate), cocamidopropyl betaine, cetyltrimethylammonium bromide (CTAB), sodium dodecylbenzenesulfonate (SDBS), sodium oleate, sodium stearate, benzalkonium chloride, sodium cocamphoacetate, sodium cocoyl glutamate, sorbitan monostearate, sorbitan trioleate, sodium lauroyl sarcosinate, stearic acid, or glyceryl stearate. In some embodiments, the surfactant is a nonionic surfactant. In some embodiments, the surfactant is polysorbate 20 or polysorbate 80. In some embodiments, the surfactant is polysorbate 80. In some embodiments, the composition comprises a surfactant at a concentration in the range of 0.005-0.5% w / v, 0.006-0.5% w / v, 0.007-0.5% w / v, 0.008-0.5% w / v, 0.009-0.5% w / v, 0.01-0.5% w / v, 0.02-0.5% w / v, 0.03- 0.5% w / v, 0.04-0.5% w / v, 0.05-0.5% w / v, 0.06-0.5% w / v, 0.07-0.5% w / v, 0.08-0.5% w / v, 0.09-0.5% w / v, 0.1-0.5% w / v, 0.2-0.5% w / v, 0.3-0.5% w / v, 0.4-0.5% w / v, 0.005-0.4% w / v, 43#14616800v20.006-0.4% w / v, 0.007-0.4% w / v, 0.008-0.4% w / v, 0.009-0.4% w / v, 0.01-0.4% w / v, 0.02- 0.4% w / v, 0.03-0.4% w / v, 0.04-0.4% w / v, 0.05-0.4% w / v, 0.06-0.4% w / v, 0.07-0.4% w / v, 0.08-0.4% w / v, 0.09-0.4% w / v, 0.1-0.4% w / v, 0.2-0.4% w / v, 0.3-0.4% w / v, 0.005-0.3% w / v, 0.006-0.3% w / v, 0.007-0.3% w / v, 0.008-0.3% w / v, 0.009-0.3% w / v, 0.01-0.3% w / v, 0.02- 0.3% w / v, 0.03-0.3% w / v, 0.04-0.3% w / v, 0.05-0.3% w / v, 0.06-0.3% w / v, 0.07-0.3% w / v, 0.08-0.3% w / v, 0.09-0.3% w / v, 0.1-0.3% w / v, 0.2-0.3% w / v, 0.005-0.2% w / v, 0.006-0.2% w / v, 0.007-0.2% w / v, 0.008-0.2% w / v, 0.009-0.2% w / v, 0.01-0.2% w / v, 0.02-0.2% w / v, 0.03-0.2% w / v, 0.04-0.2% w / v, 0.05-0.2% w / v, 0.06-0.2% w / v, 0.07-0.2% w / v, 0.08-0.2% w / v, 0.09-0.2% w / v, 0.1-0.2% w / v, 0.005-0.1% w / v, 0.006-0.1% w / v, 0.007-0.1% w / v, 0.008-0.1% w / v, 0.009-0.1% w / v, 0.01-0.1% w / v, 0.02-0.1% w / v, 0.03-0.1% w / v, 0.04-0.1% w / v, 0.05-0.1% w / v, 0.06-0.1% w / v, 0.07-0.1% w / v, 0.08-0.1% w / v, 0.09-0.1% w / v, 0.01- 0.02% w / v, 0.01-0.03% w / v, 0.01-0.04% w / v, 0.01-0.05% w / v, 0.01-0.06% w / v, 0.01-0.07% w / v, 0.01-0.08% w / v, 0.01-0.09% w / v, 0.02-0.03% w / v, 0.03-0.04% w / v, 0.04-0.05% w / v, 0.05-0.06% w / v, 0.06-0.07% w / v, or 0.07-0.08% w / v. In some embodiments, the composition comprises a surfactant at a concentration in the range of 0.05-5mg / mL, 0.06-5mg / mL, 0.07- 5mg / mL, 0.08-5mg / mL, 0.09-5mg / mL, 0.1-5mg / mL, 0.2-5mg / mL, 0.3-5mg / mL, 0.4- 5mg / mL, 0.5-5mg / mL, 0.6-5mg / mL, 0.7-5mg / mL, 0.8-5mg / mL, 0.9-5 mg / mL, l-5mg / mL, 2- 5mg / mL, 3-5mg / mL, 4-5mg / mL, 0.05-4mg / mL, 0.06-4mg / mL, 0.07-4mg / mL, 0.08-4mg / mL, 0.09-4mg / mL, 0.1-4mg / mL, 0.2-4mg / mL, 0.3-4mg / mL, 0.4-4mg / mL, 0.5-4mg / mL, 0.6- 4mg / mL, 0.7-4mg / mL, 0.8-4mg / mL, 0.9-4mg / mL, l-4mg / mL, 2-4mg / mL, 3-4mg / mL, 0.05- 3mg / mL, 0.06-3mg / mL, 0.07-3mg / mL, 0.08-3mg / mL, 0.09-3mg / mL, 0.1-3mg / mL, 0.2- 3mg / mL, 0.3-3mg / mL, 0.4-3mg / mL, 0.5-3mg / mL, 0.6-3mg / mL, 0.7-3mg / mL, 0.8-3mg / mL, 0.9-3mg / mL, l-3mg / mL, 2-3mg / mL, 0.05-2mg / mL, 0.06-2mg / mL, 0.07-2mg / mL, 0.08- 2mg / mL, 0.09-2mg / mL, 0.1-2mg / mL, 0.2-2mg / mL, 0.3-2mg / mL, 0.4-2mg / mL, 0.5-2mg / mL, 0.6-2mg / mL, 0.7-2mg / mL, 0.8-2mg / mL, 0.9-2 mg / mL, l-2mg / mL, 0.05-lmg / mL, 0.06- Img / mL, 0.07-lmg / mL, 0.08-lmg / mL, 0.09-lmg / mL, 0.1-lmg / mL, 0.2-lmg / mL, 0.3- Img / mL, 0.4-lmg / mL, 0.5-lmg / mL, 0.6-lmg / mL, 0.7-lmg / mL, 0.8-lmg / mL, 0.9-lmg / mL, 0.1-0.2mg / mL, 0.1-0.3mg / mL, 0.1-0.4mg / mL, 0.1-0.5mg / mL, 0.1-0.6mg / mL, 0.1-0.7mg / mL, 0.1-0.8mg / mL, 0.1-0.9mg / mL, 0.2-0.3mg / mL, 0.3-0.4mg / mL, 0.4-0.5mg / mL, 0.5-0.6mg / mL, 0.6-0.7mg / mL, or 0.7-0.8mg / mL.[000131] In some embodiments, the composition further comprises a sugar. In some embodiments, the composition comprises a sugar at a concentration in the range of 1-5% w / v, 1.2-5% w / v, 1.4-5% w / v, 1.6-5% w / v, 1.8-5% w / v, 2-5% w / v, 2.2-5% w / v, 2.4-5% w / v, 2.6- 5% w / v, 2.8-5% w / v, 3-5% w / v, 3.25-5% w / v, 3.5-5% w / v, 3.75-5% w / v, 4-5% w / v, 4.25-5% 44#14616800v2w / v, 4.5-5% w / v, 4.75-5% w / v, 1-1.2% w / v, 1-1.4% w / v, 1-1.6% w / v, 1-1.8% w / v, 1-2% w / v, 1-2.2% w / v, 1-2.4% w / v, 1-2.6% w / v, 1-2.8% w / v, 1-3% w / v, 1-3.25% w / v, 1-3.5% w / v, 1-3.75% w / v, 1-4% w / v, 1-4.25% w / v, 1-4.5% w / v, 1-4.75% w / v, 1.2-1.4% w / v, 1-4- 1.6% w / v, 1.6-1.8% w / v, 1.8-2% w / v, 2-2.2% w / v, 2.2-2.4% w / v, 2.4-2.6% w / v, 2.6-2.8% w / v, 2.8-3% w / v, 3-3.25% w / v, 3.25-3.5% w / v, 3.5-3.75% w / v, 3.75-4% w / v, 4-4.25% w / v, 4.25-4.5% w / v, or 4.5-4.75% w / v. In some embodiments, the composition comprises a sugar at a concentration in the range of 10-50mg / mL, 12-50mg / mL, 14-50mg / mL, 16-50mg / mL, 18-50mg / mL, 20-50mg / mL, 22-50mg / mL, 24-50mg / mL, 26-50mg / mL, 28-50mg / mL, 30- 50mg / mL, 32.5-50mg / mL, 35-50mg / mL, 37.5-50mg / mL, 40-50mg / mL, 42.5-50mg / mL, 45- 50mg / mL, 47.5-50mg / mL, 10-12mg / mL, 10-14mg / mL, 10-16mg / mL, 10-18mg / mL, 10- 20mg / mL, 10-22mg / mL, 10-24mg / mL, 10-26mg / mL, 10-28mg / mL, 10-30mg / mL, 10- 32.5mg / mL, 10-35mg / mL, 10-37.5mg / mL, 10-40mg / mL, 10-42.5mg / mL, 10-45mg / mL, 10- 47.5mg / mL, 12-14mg / mL, 14-16mg / mL, 16-18mg / mL, 18-20mg / mL, 20-22mg / mL, 22- 24mg / mL, 24-26mg / mL, 26-28mg / mL, 28-30mg / mL, 30-32.5mg / mL, 32.5-35mg / mL, 35- 37.5mg / mL, 37.5-40mg / mL, 40-42.5mg / mL, 42.5-45mg / mL, or 45-47.5mg / mL. In some embodiments, the sugar is glucose, fructose, galactose, sucrose, lactose, maltose, dextrose, ribose, xylose, mannose, arabinose, trehalose, raffinose, sorbitol, maltitol, erythritol, lactitol, isomalt, tagatose, or palatinose (isomaltulose). In some embodiments, the composition comprises sucrose.[000132] In some embodiments, the composition comprises a stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), histidine (e.g., L-histidine, L-His-HCl), polysorbate 80, sucrose, and arginine (e.g., L- arginine, L-Arg-HCl).[000133] In some embodiments, the composition comprises 175 mg / mL stress-sensitive antibody (e.g., anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L-histidine (e.g., L-His-HCl), 0.02% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, and 100 mM Arg-HCl (e.g., L-Arg-HCl) at pH = 5.6. In some embodiments, the composition comprises 175 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L- His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, and 100 mM L-Arg-HCl at pH = 5.6. In some embodiments, the composition comprises 150 mg / mL stress-sensitive antibody 45#14616800v2(e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L-histidine (e.g., L-His-HCl), 0.02% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, and 100 mM Arg-HCl (e.g., L-Arg-HCl) at pH = 5.6. In some embodiments, the composition comprises 150 mg / mL stress-sensitive antibody (e.g., an anti- TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L- His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, and 100 mM L-Arg-HCl at pH = 5.6. [000134] In some embodiments, the composition comprises 175 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-histidine (e.g., L-His-HCl), 0.2% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, 100 mM Arg-HCl (e.g., L-Arg-HCl), and 10 mM L- methionine (e.g., L-Met-HCl) at pH = 5.6. In some embodiments, the composition comprises 175 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, 100 mM L-Arg-HCl, and 10 mM L-Met-HCl at pH = 5.6.[000135] In some embodiments, the composition comprises 150 mg / mL stress-sensitive antibody (e.g., anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-histidine (e.g., L-His-HCl), 0.2% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, 100 mM Arg-HCl (e.g., L-Arg-HCl), and 10 mM L- methionine (e.g., L-Met-HCl) at pH = 5.6. In some embodiments, the composition comprises 150 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, 100 mM L-Arg-HCl, and 10 mM L-Met-HCl at pH = 5.6.[000136] In some embodiments, the composition improves stability of the stress-sensitive antibody (e.g., the anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), when the antibody is subject to thermal, agitation, and / or light stress.46#14616800v2[000137] In some embodiments, compositions disclosed herein reduce the degradation of an antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce the degradation of an antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%- 20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%- 40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%- 50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%- 50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%- 100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%- 70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000138] In some embodiments, compositions disclosed herein reduce the formation of low molecular weight degradation species by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce the formation of molecular weight degradation species by l%-100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%- 80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%- 90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%- 90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%- 80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%- 60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%- 100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000139] In some embodiments, compositions disclosed herein reduce the aggregation of an antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some 47#14616800v2embodiments, compositions disclosed herein reduce the aggregation of an antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%- 20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%- 40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%- 50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%- 50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%- 100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%- 70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000140] In some embodiments, compositions disclosed herein reduce the formation of high molecular weight aggregates by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce the formation of high molecular weight aggregates by l%-100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%- 60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000141] In some embodiments, compositions disclosed herein reduce the oxidation (e.g., di-oxidation) of an antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition. In some embodiments, compositions disclosed herein reduce the oxidation (e.g., di-oxidation) of an antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%- 20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%- 40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%- 50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%- 48#14616800v250%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%- 100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%- 70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000142] In some embodiments, compositions disclosed herein reduce the post-translational modification of an antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce the post-translational modification of an antibody by 1%-100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%- 70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%- 80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%- 80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%- 70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%- 100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%- 90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000143] In some embodiments, compositions disclosed herein reduce deamidation (e.g., asparagine deamidation) of an antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce deamidation (e.g., asparagine deamidation) of an antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).49#14616800v2[000144] In some embodiments, compositions disclosed herein reduce glycation of an antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce glycation of an antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000145] In some embodiments, compositions disclosed herein reduce formation of charged variants of antibodies by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to formation of charged variants of antibodies in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce formation of charged variants of antibodies by 1%-100%, 5%-100%, 5%-90%, 5%-80%, 5%- 70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to formation of charged variants of antibodies in a control composition (e.g., when subjected to stress).[000146] In some embodiments, compositions disclosed herein reduce formation of non- covalently modified forms of antibodies by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to formation of non-covalently modified antibodies in a 50#14616800v2control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce formation of non-covalently modified forms of antibodies by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%- 20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%- 40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%- 50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%- 50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%- 100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%- 70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to formation of non-covalently modified antibodies in a control composition (e.g., when subjected to stress).[000147] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein exhibit improved appearance (e.g., reduced changes to coloring, reduced yellowing, reduced increases in turbidity) relative to compositions comprising the same stress-sensitive antibodies formulated differently. In some embodiments, appearance of a composition is determined by visible inspection and comparison to a standard control (e.g., performed by one of skill in the art).[000148] In some embodiments, compositions disclosed herein improve the appearance of a composition comprising a stress sensitive antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein improve the appearance of a composition comprising a stress sensitive antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000149] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein preserve the color of the composition (e.g., reduce changes to 51#14616800v2the color of the composition) relative to compositions comprising the same stress-sensitive antibodies formulated differently. In some embodiments, the color of a composition is detected by visual inspection. In some embodiments, compositions comprising stresssensitive antibodies formulated as described herein reduce yellowing of the composition relative to compositions comprising the same stress-sensitive antibodies but formulated differently. In some embodiments, yellowing of a composition is detected by visual inspection. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein reduce yellowing of the composition after exposure to stress conditions relative to compositions comprising the same stress-sensitive antibodies but formulated differently and exposed to the same stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are colorless-to- pale yellow after exposure to stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are colorless after exposure to stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are pale yellow after exposure to stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are clearer and / or less yellow after exposure to stress conditions relative to compositions comprising the same stress-sensitive antibodies but formulated differently and exposed to the same stress conditions.[000150] In some embodiments, compositions disclosed herein preserve the color of a composition comprising a stress sensitive antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein preserve the color of a composition comprising a stress sensitive antibody by 1%- 100%, 5%-100%, 5%- 90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%- 100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%- 20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%- 30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%- 100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%- 80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%- 90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).52#14616800v2[000151] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein reduce darkening of the composition relative to compositions comprising the same stress-sensitive antibodies but formulated differently. In some embodiments, darkening of a composition is detected by visual inspection. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein reduce darkening of the composition after exposure to stress conditions relative to compositions comprising the same stress-sensitive antibodies but formulated differently and exposed to the same stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are colorless after exposure to stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are lighter or clearer after exposure to stress conditions than compositions comprising the same stress-sensitive antibodies but formulated differently and exposed to the same stress conditions.[000152] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein reduce turbidity relative to compositions comprising the same stress-sensitive antibodies formulated differently. In some embodiments, the turbidity of a solution is detected by visual inspection. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein reduce turbidity of the composition after exposure to stress conditions relative to compositions comprising the same stresssensitive antibodies but formulated differently and exposed to the same stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are clear after exposure to stress conditions. In some embodiments, compositions comprising stress-sensitive antibodies formulated as described are less turbid after exposure to stress conditions relative to compositions comprising the same stress-sensitive antibodies but formulated differently and exposed to the same stress conditions.[000153] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein reduce visible particle formation relative to compositions comprising the same stress-sensitive antibodies formulated differently. In some embodiments, compositions disclosed herein reduce visible particle formation by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce visible particle formation by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%- 53#14616800v270%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to a control composition (e.g., when subjected to stress).[000154] In some embodiments, compositions disclosed herein reduce the level of sub- visible particles in a composition comprising a stress sensitive antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce the level of sub-visible particles in a composition comprising a stress sensitive antibody by l%-100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%- 60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%- 70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%- 70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%- 60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%- 90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000155] In some embodiments, compositions disclosed herein maintains a level of sub- visible particles in a composition comprising a stress sensitive antibody to less than 1000 counts / mL, less than 900 counts / mL, less than 800 counts / mL, less than 700 counts / mL, less than 600 counts / mL, less than 500 counts / mL, less than 400 counts / mL, less than 300 counts / mL, less than 200 counts / mL, or less than 100 counts / mL.[000156] In some embodiments, compositions disclosed herein reduce the viscosity of a composition comprising a stress sensitive antibody by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to the antibody in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce the 54#14616800v2viscosity of a composition comprising a stress sensitive antibody by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to the antibody in a control composition (e.g., when subjected to stress).[000157] In some embodiments, compositions comprising stress-sensitive antibodies formulated as described herein prevent reduction in antibody concentration over a period of time (e.g., 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, 7 days, a week, 2 weeks, 3 weeks, 4 weeks, 5 weeks, 6 weeks, 7 weeks, 8 weeks, 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 1 year, or more) relative to compositions comprising the same stresssensitive antibodies formulated differently. In some embodiments, compositions disclosed herein reduce loss of antibody concentration by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to antibody concentration in a control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce loss of antibody concentration by 1%- 100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%- 60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to antibody concentration in a control composition (e.g., when subjected to stress).[000158] In some embodiments, compositions disclosed herein reduce formation of covalently modified forms of antibodies by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% relative to formation of covalently modified antibodies in a 55#14616800v2control composition (e.g., when subjected to stress). In some embodiments, compositions disclosed herein reduce formation of covalently modified forms of antibodies by 1%-100%, 5%-100%, 5%-90%, 5%-80%, 5%-70%, 5%-60%, 5%-50%, 5%-40%, 5%-30%, 5%-20%, 5%-10%, 10%-100%, 10%-90%, 10%-80%, 10%-70%, 10%-60%, 10%-50%, 10%-40%, 10%-30%, 10%-20%, 20%-100%, 20%-90%, 20%-80%, 20%-70%, 20%-60%, 20%-50%, 20%-40%, 20%-30%, 30%-100%, 30%-90%, 30%-80%, 30%-70%, 30%-60%, 30%-50%, 30%-40%, 40%-100%, 40%-90%, 40%-80%, 40%-70%, 40%-60%, 40%-50%, 50%-100%, 50%-90%, 50%-80%, 50%-70%, 50%-60%, 60%-100%, 60%-90%, 60%-80%, 60%-70%, 70%-100%, 70%-90%, 70%-80%, 80%-100%, 80%-90%, or 90%-100% relative to formation of covalently modified antibodies in a control composition (e.g., when subjected to stress). [000159] In some embodiments, the compositions disclosed herein are formulated to have a specific tonicity (e.g., hypertonicity) across a cell membrane. As used herein, the term “tonicity” refers to the relative concentration of non-permeable solutes dissolved in a solution compared to another solution, separated by a semi-permeable membrane (e.g., a cell membrane). Tonicity is equal to the sum of the concentrations of the solutes which have the capacity to exert an osmotic force across the membrane, and involves only non-permeable molecules. In contrast, osmolality involves both permeable and non-permeable molecules and is a measure of the osmotic pressure of a solution. In some embodiments, a composition comprises an excipient to adjust tonicity or osmolality of a solution, or a lyoprotectant for lyophilized powders. In some embodiments, an excipient is an ionic tonicity-adjusting excipient (e.g., sodium chloride). In some embodiments, an excipient is a non-ionic osmolality-adjusting excipient (e.g., sucrose, trehalose, mannitol, maltose, or sorbitol). In some embodiments, a lyoprotectant is trehalose or sucrose. In some embodiments, an excipient (e.g., sodium chloride or arginine) also modulates the viscosity of a composition. In some embodiments, the osmolality of a composition comprising a stress-sensitive antibody is about 250-350 mOsm / kg, about 275-350 mOsm / kg, about 300-350 mOsm / kg, about 325-350 mOsm / kg, about 250-275 mOsm / kg, about 250-300 mOsm / kg, about 250-325 mOsm / kg, about 275-300 mOsm / kg, or about 300-325 mOsm / kg. In some embodiments, the osmolality of a composition comprising a stress-sensitive antibody is at least 200 mOsm / kg, at least 220 mOsm / kg, at least 240 mOsm / kg, at least 260 mOsm / kg, at least 280 mOsm / kg, at least 300 mOsm / kg, at least 325 mOsm / kg, at least 350 mOsm / kg, at least 375 mOsm / kg, or at least 400 mOsm / kg. In some embodiments, the osmolality of a composition comprising a stresssensitive antibody is 300 mOsm / kg.56#14616800v2[000160] In some embodiments, the present disclosure provides a vial comprising a composition described herein. In some embodiments, the vial is a glass vial. Any suitable glass vials for housing an antibody composition can be used with the antibody composition described herein. Non-limiting examples of vials include but are not limited to borosilicate glass vial, soda lime glass vial, Pyrex glass vial, or amber glass vial. In some embodiments, the vial is a borosilicate glass vial. In some embodiments, the vial is a ISO 2R glass vial. [000161] In some embodiments, the present disclosure provides a prefilled syringe comprising a composition described herein. Any suitable syringe can be prefilled with the composition described herein. In some embodiments, a prefilled syringe is a glass syringe (e.g., a BD Neopak standard syringe). In some embodiments, a prefilled syringe is a silicon syringe (e.g., a BD Neopak cross-linked silicon (XSi)). In some embodiments, the syringe is an autoinjector.[000162] In some embodiments, the present disclosure provides an autoinjector comprising a composition described herein. Any suitable autoinjector can be used to house the composition described herein. In some embodiments, the autoinjector is a YPSomed autoinjector. In other embodiments, the autoinjector is a YPSomed YPSomate 2.25 mL autoinjector.[000163] In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising a stresssensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), histidine (e.g., L-histidine, L-His-HCl), polysorbate 80, sucrose, and arginine (e.g., L-arginine, L-Arg-HCl).[000164] In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 175 mg / mL stress-sensitive antibody (e.g., anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L-histidine (e.g., L-His-HCl), 0.02% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, and 100 mM Arg-HCl (e.g., L- Arg-HCl) at pH = 5.6. In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 175 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L-His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, and 100 mM L- Arg-HCl at pH = 5.6.57#14616800v2[000165] In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 150 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L-histidine (e.g., L-His-HCl), 0.02% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, and 100 mM Arg-HCl (e.g., L- Arg-HCl) at pH = 5.6. In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 150 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 100 mM L-His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, and 100 mM L- Arg-HCl at pH = 5.6.[000166] In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 175 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-histidine (e.g., L-His-HCl), 0.2% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, 100 mM Arg-HCl (e.g., L- Arg-HCl), and 10 mM L-methionine (e.g., L-Met-HCl) at pH = 5.6. In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 175 mg / mL stress-sensitive antibody (e.g., an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, 100 mM L-Arg-HCl, and 10 mM L-Met-HCl at pH = 5.6.[000167] In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 150 mg / mL stress-sensitive antibody (e.g., anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-histidine (e.g., L-His-HCl), 0.2% w / v (e.g., 0.2mg / mL) polysorbate 80, 2% w / v (e.g., 20mg / mL) sucrose, 100 mM Arg-HCl (e.g., L- Arg-HCl), and 10 mM L-methionine (e.g., L-Met-HCl) at pH = 5.6. In some embodiments, the present disclosure provides a vial, prefilled syringe (e.g., a prefilled glass syringe), or autoinjector comprising a composition comprising 150 mg / mL stress-sensitive antibody (e.g.,58#14616800v2an anti-TMPRSS6 antibody comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53), 50 mM L-His-HCl, 0.2mg / mL polysorbate 80, 20mg / mL sucrose, 100 mM L-Arg-HCl, and 10 mM L-Met-HCl at pH = 5.6.III. Anti-TMPRSS6 Antibodies[000168] In some aspects, a stress-sensitive antibody is an anti-TMPRSS6 antibody (e.g., any one of the anti-TMPRSS6 antibody described herein). In some embodiments, an anti- TMPRSS6 antibody is sensitive to light stress (e.g., visible light and / or UV light). In some embodiments, an anti-TMPRSS6 antibody is sensitive to thermal stress (e.g., heat, freezethaw cycles). In some embodiments, an anti-TMPRSS6 antibody is sensitive to agitation stress (e.g., spinning). In some embodiments, an anti-TMPRSS6 antibody undergoes physical changes when subjected to light and / or thermal stress. In some embodiments, an anti-TMPRSS6 antibody undergoes physical changes when subjected to light, thermal, and / or agitation stress. In some embodiments, an anti-TMPRSS6 antibody undergoes degradation and / or aggregation when subjected to light, thermal, and / or agitation stress. In some embodiments, an anti-TMPRSS6 antibody undergoes chemical changes when subjected to light, thermal, and / or agitation stress. In some embodiments, an anti-TMPRSS6 antibody undergoes post-translational modifications (e.g., oxidation, deamidation and / or glycation) when subjected to light, thermal, and / or agitation stress. In some embodiments, an anti- TMPRSS6 antibody undergoes oxidation when subjected to light, thermal, and / or agitation stress. In some embodiments, an anti-TMPRSS6 comprising a heavy chain having the amino acid sequence of SEQ ID NO: 52 and a light chain having the amino acid sequence of SEQ ID NO: 53 is a stress-sensitive antibody.[000169] In some embodiments, the anti-TMPRSS6 antibody is an antibody specific for TMPRSS6. Provided herein, in some aspects, are antibodies that bind to human TMPRSS6 with high specificity and affinity. In some embodiments, the anti-TMPRSS6 antibody described herein specifically binds to any extracellular epitope of a TMPRSS6 or an epitope that becomes exposed to an antibody. In some embodiments, anti-TMPRSS6 antibodies provided herein bind specifically to TMPRSS6 from human, non-human primates, mouse, rat, etc. In some embodiments, anti-TMPRSS6 antibodies provided herein bind to human TMPRSS6. In some embodiments, the anti-TMPRSS6 antibody described herein binds to an amino acid segment of a human or non-human primate TMPRSS6. In some embodiments, the59#14616800v2anti-TMPRSS6 antibody described herein specifically binds to an epitope on human TMPRSS6.[000170] TMPRSS6, also called Matriptase-2, is a serine protease within the type II transmembrane serine protease (TTSP) family. Enzymes in this family share common structural features, including a serine protease domain, a variable length stem region comprising a mosaic of structural domains, and a short cytoplasmic tail (Hooper et al., Type II transmembrane serine proteases: Insights into an emerging class of cell surface proteolytic enzymes. J Biol Chem. 2001; 276:857-60). The TTSP family of proteases comprises multiple sub-families, including the matriptase sub-family, which comprises TMPRSS 2-5. TMPRSS6, to which the antibodies of some embodiments of the present disclosure specifically bind, is highly conserved across mammalian species. In some embodiments, the antibodies of the present disclosure specifically bind a TMPRSS6 protein encoded by a human TMPRSS6 gene (e.g., GenBank: AAH39082.1, e.g., NCBI Gene ID: 164656). In some embodiments, the antibodies of the present disclosure specifically bind a TMPRSS6 protein encoded by a mouse TMPRSS6 gene (e.g., GenBank: AAH57674.1, e.g., NCBI Gene ID: 71753). In other embodiments, the antibodies of the present disclosure specifically bind a TMPRSS6 protein encoded by a non-human primate TMPRSS6 gene (e.g., cynomolgus monkey (i.e., Macaca fascicularis), e.g., NCBI Gene ID: 102139590). The TMPRSS6 gene spans 18 exons with 17 intervening introns, with the matriptase-2 protein domain boundaries corresponding with intron / exon junctions of the encoding gene across all species. Structurally, matriptase-2 comprises canonical TTSP features, such as a short cytoplasmic amino terminal tail, a transmembrane region, a stem region containing two complement protein subcomponents (Clr / Cls, urchin embryonic growth factor and bone morphogenic protein 1 (CUB) domains), and three low-density lipoprotein receptor class A (LDLR) domains, as well as a trypsin-like serine protease domain at the carboxy terminus. All of these structural features are tightly conserved across human, macaque, dog, cow, mouse and rat, with the human protein sharing 95.6%, 91.1%, 85.6%, 80.1% and 80.4% identity, respectively, to matriptase-2 from these species (Ramsay et al., The type II transmembrane serine protease matriptase-2 — identification, structural features, enzymology, expression pattern and potential roles. Front Biosci. 2008; 13:259-79).[000171] The matriptase-2 proteolytic domain comprises a serine protease triad of H, D and S residues required for catalytic activity, and an SWG motif predicted to be located at the top of the substrate SI binding pocket positioning the scissile bond of the substrate in the correct orientation. Proteolytic activation of matriptase-2 is predicted to occur within a motif 60#14616800v2(RIVGG) at the junction of the pro- and catalytic domains, which is characteristic of serine proteases and conserved across species (Velasco et al., Matriptase-2, a membrane-bound mosaic serine proteinase predominantly expressed in human liver and showing degrading activity against extracellular matrix proteins. J Biol Chem. 2002; 277:37637-46). In adult human and mouse tissues, the primary site of matriptase-2 mRNA expression is the liver. Specifically, matriptase-2 mRNA expression has been demonstrated to be restricted to liver hepatocytes.[000172] Functionally, matriptase-2 acts to cleave hemojuvelin (HJV), a protein essential in the process of iron regulation through its positive regulation of hepcidin expression. Hepcidin is a known negative regulator of iron absorption, release, and recycling. In the absence of matriptase-2, HJV levels are increased, leading to increased levels of hepcidin and consequently inhibition of iron transport. The establishment of matriptase-2 as an essential component of iron homeostasis was based on phenotypes of iron-refractory iron deficiency anemia in human patients with loss-of-function TMPRSS6 mutations (Cui et al., Iron- refractory iron deficiency anemia: new molecular mechanisms. Kidney Int. 2009;76(11): 1137-1141). Thus, in some embodiments, the antibodies of the present disclosure inhibit matriptase-2 activity in order to regulate iron homeostasis. In some embodiments, the antibodies of the present disclosure inhibit matriptase-2 activity to decrease iron transport through increased hepcidin activity.[000173] In some embodiments, the anti-TMPRSS6 antibody described herein may bind to a fragment of a human TMPRSS6. The fragment of TMPRSS6 may be between about 5 and about 425 amino acids, between about 10 and about 400 amino acids, between about 50 and about 350 amino acids, between about 100 and about 300 amino acids, between about 150 and about 250 amino acids, between about 200 and about 300 amino acids, or between about 75 and about 150 amino acids in length. In some embodiments, the fragment may comprise a contiguous number of amino acids from TMPRSS6. In other embodiments, the fragment may comprise a non-contiguous number of amino acids from TMPRSS6.[000174] In some embodiments, the anti-TMPRSS6 antibodies disclosed herein specifically bind to mouse TMPRSS6. In some embodiments, the anti-TMPRSS6 antibodies disclosed herein specifically bind rat TMPRSS6. In some embodiments, the anti-TMPRSS6 antibodies disclosed herein specifically bind non-human primate TMPRSS6 (e.g., TMPRSS6 from cynomolgus monkey, rhesus monkey, African green monkey, vervet monkey, squirrel monkey, owl monkey, pig-tailed monkey, or baboon). In some embodiments, the anti- TMPRSS6 antibodies disclosed herein specifically bind to human TMPRSS6.61#14616800v2[000175] In some embodiments, the anti-TMPRSS6 antibodies described herein are affinity matured clones. In some embodiments, an anti-TMPRSS6 antibody specifically binds a TMPRSS6 (e.g., a human or non-human primate TMPRSS6) with binding affinity (e.g., as indicated by KD) of at least about IO’4M, 10’5M, IO’6M, IO’7M, 8’7M, 6’7M, 4’7M, 2’7M, IO’8M, 8'8M, 6'8M, 4'8M, 2’8M, IO’9M, IO’10M, IO’11M, IO’12M, IO’13M, or less. For example, the anti-TMPRSS6 antibodies of the present disclosure can bind to a TMPRSS6 protein (e.g., human TMPRSS6) with an affinity between 5 pM and 750 nM, e.g., between 1 nM and 500 nM, e.g., between 10 nM and 450 nM, e.g., between 50 pM and 100 nM, e.g., between 500 pM and 50 nM. The disclosure also includes antibodies that compete with any of the antibodies described herein for binding to a TMPRSS6 protein (e.g., human TMPRSS6) and that have an affinity of 500 nM or lower (e.g, 400 nM or lower, 100 nM or lower, 80 nM or lower, 50 nM or lower, 20 nM or lower, 10 nM or lower, 500 pM or lower, 50 pM or lower, or 5 pM or lower). In some embodiments, the anti-TMPRSS6 antibodies described herein binds to TMPRSS6 with a KD of sub-nanomolar range.[000176] The affinity and binding kinetics of the anti-TMPRSS6 antibody can be tested using any suitable method, for example, binding affinity (or binding specificity) can be determined by a variety of methods including, but not limited to, biosensor technology (e.g., OCTET or BIACORE), equilibrium dialysis, equilibrium binding, gel filtration, ELISA, surface plasmon resonance (SPR), fluorescent activated cell sorting (FACS) or spectroscopy (e.g., using a fluorescence assay). Exemplary conditions for evaluating binding affinity are in HbS-P buffer (10 mM HEPES pH7.4, 150 mM NaCl, 0.005% (v / v) surfactant P20) and PBS buffer (lOmM PO4-3, 137mM NaCl, and 2.7mM KC1). These techniques can be used to measure the concentration of bound proteins as a function of target protein concentration. The concentration of bound protein ([[Bound]]) is generally related to the concentration of free target protein ([[Free]]) by the following equation:[[Bound]] = [[Free]] / (Kd+[[Free]])[000177] It is not always necessary to make an exact determination of KA, though, since sometimes it is sufficient to obtain a quantitative measurement of affinity, e.g., determined using a method such as ELISA or FACS analysis, is proportional to KA, and thus can be used for comparisons, such as determining whether a higher affinity is, e.g., 2-fold higher, to obtain a qualitative measurement of affinity, or to obtain an inference of affinity, e.g., by activity in a functional assay, e.g., an in vitro or in vivo assay.[000178] The heavy chain (HC) and light chain (LC) sequences, heavy chain variable domain (VH) and light chain variable domain (VL), CDR sequences, and heavy chain and 62#14616800v2light chain constant region sequences of non-limiting examples of anti-TMPRSS6 antibodies are provided in Table 1.Table 1. Examples of anti-TMPRSS6 antibodies (CDRs according to the Kabat definition)63#14616800v264#14616800v265#14616800v266#14616800v267#14616800v2[000179] In some embodiments, the anti-TMPRSS6 antibodies of the present disclosure comprise one or more of the HC CDRs (e.g., HC CDR1, HC CDR2, or HC CDR3) amino acid sequences from any one of the anti-TMPRSS6 antibodies selected from Table 1. In some embodiments, the anti-TMPRSS6 antibodies of the present disclosure comprise the HC CDR1, HC CDR2, and HC CDR3 as provided for any one of the antibodies elected from Table 1. In some embodiments, the anti-TMPRSS6 antibodies of the present disclosure comprise one or more of the LC CDRs (e.g., LC CDR1, LC CDR2, or LC CDR3) amino acid sequences from any one of the anti-TMPRSS6 antibodies selected from Table 1. In some embodiments, the anti-TMPRSS6 antibodies of the present disclosure comprise the LC CDR1, LC CDR2, and LC CDR3 s provided for any one of the anti-TMPRSS6 antibodies selected from Table 1.[000180] In some embodiments, the anti-TMPRSS6 antibodies of the present disclosure comprises the HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and LC CDR3 as provided for any one of the anti-TMPRSS6 antibodies selected from Table 1. In some embodiments, antibody heavy and light chain CDR3 domains may play a particularly important role in the binding specificity / affinity of an antibody for an antigen. Accordingly, the anti-TMPRSS6 antibodies of the disclosure may include at least the heavy and / or light chain CDR3s of any one of the anti-TMPRSS6 antibodies selected from Table 1.68#14616800v2[000181] In some embodiments, the anti-TMPRSS6 antibody comprises a heavy chain variable region that comprises a heavy chain CDR1 (HC CDR1), a heavy chain CDR2 (HC CDR2), and a heavy chain CDR3 (HC CDR3). In some embodiments, the anti-TMPRSS6 antibody comprises a light chain variable region that comprises a light chain CDR1 (LC CDR1), a light chain CDR2 (LC CDR2), and a light chain CDR3 (LC CDR3).[000182] Also within the scope of the present disclosure are functional variants of any of the exemplary anti-TMPRSS6 antibodies as disclosed herein. A functional variant may contain one or more amino acid residue variations in the VH and / or VL, or in one or more of the HC CDRs and / or one or more of the LC CDRs as relative to the reference antibody, while retaining substantially similar binding and biological activities (e.g., substantially similar binding affinity, binding specificity, inhibitory activity, or a combination thereof) as the reference antibody.[000183] In some embodiments, any of the anti-TMPRSS6 antibodies of the disclosure have one or more CDRs (e.g., HC CDR or LC CDR) sequences substantially similar to any of the HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 sequences from one of the anti-TMPRSS6 antibodies selected from Table 1. In some embodiments, the position of one or more CDRs along the VH (e.g, HC CDR1, HC CDR2, or HC CDR3) and / or VL (e.g., LC CDR1, LC CDR2, or LC CDR3) region of an antibody described herein can vary by one, two, three, four, five, or six amino acid positions so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% of the binding of the original antibody from which it is derived). For example, in some embodiments, the position defining a CDR of any antibody described herein can vary by shifting the N-terminal and / or C-terminal boundary of the CDR by one, two, three, four, five, or six amino acids, relative to the CDR position of any one of the antibodies described herein, so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% of the binding of the original antibody from which it is derived). In another embodiment, the length of one or more CDRs along the VH (e.g., HC CDR1, HC CDR2, or HC CDR3) and / or VL (e.g, LC CDR1, LC CDR2, or LC CDR3) region of an antibody described herein can vary (e.g., be shorter or longer) by one, two, three, four, five, or more amino acids, so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at69#14616800v2least 60%, at least 70%, at least 80%, at least 90%, at least 95% of the binding of the original antibody from which it is derived).[000184] Accordingly, in some embodiments, a HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 described herein may be one, two, three, four, five or more amino acids shorter than one or more of the CDRs described herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). In some embodiments, a HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 described herein may be one, two, three, four, five or more amino acids longer than one or more of the CDRs described herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). In some embodiments, the amino portion of a HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 described herein can be extended by one, two, three, four, five or more amino acids compared to one or more of the CDRs described herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). In some embodiments, the carboxy portion of a HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 described herein can be extended by one, two, three, four, five or more amino acids compared to one or more of the CDRs described herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). In some embodiments, the amino portion of a HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 described herein can be shortened by one, two, three, four, five or more amino acids compared to one or more of the CDRs described herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g.,70#14616800v2substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). In some embodiments, the carboxy portion of a HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and / or LC CDR3 described herein can be shortened by one, two, three, four, five or more amino acids compared to one or more of the CDRs described herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). Any method can be used to ascertain whether immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained, for example, using binding assays and conditions described in the art.[000185] In some examples, any of the anti-TMPRSS6 antibodies of the disclosure have one or more CDR (e.g., HC CDR or LC CDR) sequences substantially similar to any one of the anti-TMPRSS6 antibodies selected from Table 1. For example, the antibodies may include one or more CDR sequence(s) from any of the anti-TMPRSS6 antibodies selected from Table 1 containing up to 5, 4, 3, 2, or 1 amino acid residue variations as compared to the corresponding CDR region in any one of the CDRs provided herein (e.g., CDRs from any of the anti-TMPRSS6 antibodies selected from Table 1) so long as immunospecific binding to TMPRSS6 (e.g., human TMPRSS6) is maintained (e.g., substantially maintained, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% relative to the binding of the original antibody from which it is derived). In some embodiments, any of the amino acid variations in any of the CDRs provided herein may be conservative variations. Conservative variations can be introduced into the CDRs at positions where the residues are not likely to be involved in interacting with a TMPRSS6 protein (e.g., a human TMPRSS6 protein), for example, as determined based on a crystal structure. Some aspects of the disclosure provide anti-TMPRSS6 antibodies that comprise one or more of the heavy chain variable (VH) and / or light chain variable (VL) domains provided herein. In some embodiments, any of the VH domains provided herein include one or more of the HC CDR sequences (e.g., HC CDR1, HC CDR2, and HC CDR3) provided herein, for example, any of the CDR-H sequences provided in any one of the anti-TMPRSS6 selected from Table 1. In some embodiments, any of the VL domains provided herein include one or more of the CDR- L sequences (e.g., LC CDR1, LC CDR2, and LC CDR3) provided herein, for example, any of71#14616800v2the LC CDR sequences provided in any one of the anti-TMPRSS6 antibodies selected from Table 1.[000186] In some embodiments, an anti-TMPRSS6 antibody of the disclosure include any antibody that includes a heavy chain variable domain and / or a light chain variable domain of any one of the anti-TMPRSS6 antibodies selected from Table 1, and variants thereof. In some embodiments, anti-TMPRSS6 antibodies of the disclosure include any antibody that includes the heavy chain variable and light chain variable pairs of any anti-TMPRSS6 antibodies selected from Table 1.[000187] Aspects of the disclosure provide anti-TMPRSS6 antibodies having a heavy chain variable (VH) and / or a light chain variable (VL) domain amino acid sequence homologous to any of those described herein. In some embodiments, the anti-TMPRSS6 antibody comprises a heavy chain variable sequence or a light chain variable sequence that is at least 75% (e.g, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the heavy chain variable sequence and / or any light chain variable sequence of any one of the anti- TMPRSS6 antibodies selected from Table 1. In some embodiments, a heavy chain variable and / or a light chain variable amino acid sequences do not vary within any of the CDR sequences provided herein. For example, in some embodiments, the degree of sequence variation (e.g, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a heavy chain variable and / or a light chain variable sequence excluding any of the CDR sequences provided herein. In some embodiments, any of the anti- TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence and a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of any anti-TMPRSS6 antibodies selected from Table 1.[000188] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure is an antibody comprising a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH of any of the anti-TMPRSS6 antibodies listed in Table 1. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure is a humanized antibody comprising a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid 72#14616800v2variation) as compared with the VL of any one of the anti-TMPRSS6 antibodies listed in Table 1. In some embodiments, a heavy chain variable and / or a light chain variable amino acid sequences do not vary within any of the CDR sequences provided herein. For example, in some embodiments, the number of amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a heavy chain variable and / or a light chain variable sequence excluding any of the CDR sequences provided herein. In some embodiments, any of the anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of any one of anti- TMPRSS6 antibodies selected from Table 1 and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of any one of anti-TMPRSS6 antibodies selected from Table 1.[000189] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure is a humanized antibody (e.g., a humanized variant containing one or more CDRs of Table 1). In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, a HC CDR3, a LC CDR1, a LC CDR2, and a LC CDR3 that are the same as the HC CDR1, HC CDR2, HC CDR3, LC CDR1, LC CDR2, and LC CDR3 shown in Table 1, and comprises a humanized heavy chain variable region and / or a humanized light chain variable region. In some embodiments, a humanized heavy chain variable and / or a humanized light chain variable amino acid sequences do not vary within any of the CDR sequences provided herein. For example, in some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a heavy chain variable and / or a light chain variable sequence excluding any of the CDR sequences provided herein. In some embodiments, a humanized anti-TMPRSS6 antibody provided herein comprises a heavy chain variable sequence and a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of any anti-TMPRSS6 antibodies selected from Table 1. In some embodiments, a humanized heavy chain variable and / or a humanized light chain variable amino acid sequences do not vary within any of the CDR sequences provided herein. For example, in73#14616800v2some embodiments, the number of amino acid variations e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a heavy chain variable and / or a light chain variable sequence excluding any of the CDR sequences provided herein. In some embodiments, a humanized anti-TMPRSS6 antibody provided herein comprises a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of any one of anti- TMPRSS6 antibodies selected from Table 1 and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of any one of anti-TMPRSS6 antibodies selected from Table 1.[000190] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, HC CDR2 and HC CDR3 of a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 7. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, LC CDR2 and LC CDR3 of a light chain variable domain having the amino acid sequence of SEQ ID NO: 8.[000191] In some embodiments, according to the Kabat definition system, an anti- TMPRSS6 antibody of the present disclosure comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 1, a HC CDR2 having the amino acid sequence of SEQ ID NO: 2, a HC CDR3 having the amino acid sequence of SEQ ID NO: 3, a LC CDR1 having the amino acid sequence of SEQ ID NO: 4, a LC CDR2 having the amino acid sequence of RAN, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000192] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 1, HC CDR2 having the amino acid sequence of SEQ ID NO: 2, and HC CDR3 having the amino acid sequence of SEQ ID NO: 3. “Collectively,” as used anywhere in the present disclosure, means that the total number of amino acid variations in all of the three heavy chain CDRs is within the defined range. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2 or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 4,74#14616800v2LC CDR2 having the amino acid sequence of RAN, and LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000193] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 1, HC CDR2 having the amino acid sequence of SEQ ID NO: 2, and HC CDR3 having the amino acid sequence of SEQ ID NO: 3. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the to the LC CDR1 having the amino acid sequence of SEQ ID NO: 4, LC CDR2 having the amino acid sequence of RAN, and LC CDR3 having the amino acid sequence of SEQ ID NO: 6. [000194] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 1; a HC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR2 having the amino acid sequence of SEQ ID NO: 2; and / or a HC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR3 having the amino acid sequence of SEQ ID NO: 3. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 4; a LC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR2 having the amino acid sequence of RAN; and / or a LC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000195] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 1; a HC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at 75#14616800v2least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR2 having the amino acid sequence SEQ ID NO: 2; and / or a HC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR3 having the amino acid sequence of SEQ ID NO: 3. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR1 having the amino acid sequence of SEQ ID NO: 4; a LC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR2 having the amino acid sequence of RAN; and / or a LC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000196] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising the amino acid sequence of SEQ ID NO: 7. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising the amino acid sequence of SEQ ID NO: 8.[000197] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19,18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH as set forth in SEQ ID NO: 7. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VL as set forth in SEQ ID NO: 8. In some embodiments, the number of amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a VH of SEQ ID NO: 7 and / or a VL of SEQ ID NO: 8 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20,19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of SEQ ID NO: 7, and / or a light chain variable sequence that76#14616800v2comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14,13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of SEQ ID NO: 8.[000198] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the VH as set forth in SEQ ID NO: 7. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the VL as set forth in SEQ ID NO: 8. In some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a VH of SEQ ID NO: 7, and / or a VL of SEQ ID NO: 8 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibody provided herein comprise a heavy chain variable sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VH of SEQ ID NO: 7, and / or a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VL of SEQ ID NO: 8.[000199] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, HC CDR2 and HC CDR3 of a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 19 or 78. Alternatively or in addition, the anti- TMPRSS6 antibody of the present disclosure comprises a LC CDR1, LC CDR2 and LC CDR3 of a light chain variable domain having the amino acid sequence of SEQ ID NO: 20. [000200] In some embodiments, according to the Kabat definition system, an anti- TMPRSS6 antibody of the present disclosure comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 13, a HC CDR2 having the amino acid sequence of SEQ ID NO:14, a HC CDR3 having the amino acid sequence of SEQ ID NO: 15, a LC CDR1 having the amino acid sequence of SEQ ID NO: 16, a LC CDR2 having the amino acid sequence of WAF, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 18.77#14616800v2[000201] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 13, HC CDR2 having the amino acid sequence of SEQ ID NO: 14, and HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2 or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 16, LC CDR2 having the amino acid sequence of WAF, and LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000202] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 13, HC CDR2 having the amino acid sequence of SEQ ID NO: 14, and HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the to the LC CDR1 having the amino acid sequence of SEQ ID NO: 16, LC CDR2 having the amino acid sequence of WAF, and LC CDR3 having the amino acid sequence of SEQ ID NO: 18. [000203] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 13; a HC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR2 having the amino acid sequence of SEQ ID NO: 14; and / or a HC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti- TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 16; a LC CDR2 having no78#14616800v2more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR2 having the amino acid sequence of WAF; and / or a LC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000204] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 13; a HC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR2 having the amino acid sequence SEQ ID NO: 14; and / or a HC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR1 having the amino acid sequence of SEQ ID NO: 16; a LC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR2 having the amino acid sequence of WAF; and / or a LC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000205] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising the amino acid sequence of SEQ ID NO: 19 or 78. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising the amino acid sequence of SEQ ID NO: 20.[000206] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH as set forth in SEQ ID NO: 19 or 78. Alternatively or in addition, the anti- 79#14616800v2TMPRSS6 antibody of the present disclosure comprises a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VL as set forth in SEQ ID NO: 20. In some embodiments, the number of amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a VH of SEQ ID NO: 19 or 78, and / or a VL of SEQ ID NO: 20 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of SEQ ID NO: 19 or 78, and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of SEQ ID NO: 20.[000207] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the VH as set forth in SEQ ID NO: 19 or 78. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the VL as set forth in SEQ ID NO: 20. In some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a VH of SEQ ID NO: 19 or 78, and / or a VL of SEQ ID NO: 20 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibody provided herein comprise a heavy chain variable sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VH of SEQ ID NO: 19 or 78, and / or a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VL of SEQ ID NO: 20.80#14616800v2[000208] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, HC CDR2 and HC CDR3 of a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 30. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, LC CDR2 and LC CDR3 of a light chain variable domain having the amino acid sequence of SEQ ID NO: 31.[000209] In some embodiments, according to the Kabat definition system, an anti- TMPRSS6 antibody of the present disclosure comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 24, a HC CDR2 having the amino acid sequence of SEQ ID NO:25, a HC CDR3 having the amino acid sequence of SEQ ID NO: 26, a LC CDR1 having the amino acid sequence of SEQ ID NO: 27, a LC CDR2 having the amino acid sequence of WAT, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000210] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 24, HC CDR2 having the amino acid sequence of SEQ ID NO: 25, and HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2 or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 27, LC CDR2 having the amino acid sequence of WAT, and LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000211] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 24, HC CDR2 having the amino acid sequence of SEQ ID NO: 25, and HC CDR3 having the amino acid sequence of SEQ ID NO:26. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the to the LC CDR1 having the amino acid sequence of SEQ ID NO: 27, LC CDR2 having the amino acid sequence of WAT, and LC CDR3 having the amino acid sequence of SEQ ID NO: 29.81#14616800v2[000212] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 24; a HC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR2 having the amino acid sequence of SEQ ID NO: 25; and / or a HC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti- TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 27; a LC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR2 having the amino acid sequence of WAT; and / or a LC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000213] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 24; a HC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR2 having the amino acid sequence SEQ ID NO: 25; and / or a HC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR1 having the amino acid sequence of SEQ ID NO: 27; a LC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR2 having the amino acid sequence of WAT; and / or a LC CDR3 that is at least 80% (e.g., at least 80%, at least82#14616800v285%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000214] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising the amino acid sequence of SEQ ID NO: 30. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising the amino acid sequence of SEQ ID NO: 31.[000215] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19,18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH as set forth in SEQ ID NO: 30. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VL as set forth in SEQ ID NO: 31. In some embodiments, the number of amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a VH of SEQ ID NO: 30 and / or a VL of SEQ ID NO: 31 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20,19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of SEQ ID NO: 30, and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of SEQ ID NO: 31.[000216] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the VH as set forth in SEQ ID NO: 30. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the VL as set forth in SEQ ID NO: 31. In some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at 83#14616800v2least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a VH of SEQ ID NO: 30, and / or a VL of SEQ ID NO: 31 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibody provided herein comprise a heavy chain variable sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VH of SEQ ID NO: 30, and / or a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VL of SEQ ID NO: 31.[000217] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, HC CDR2 and HC CDR3 of a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 37. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, LC CDR2 and LC CDR3 of a light chain variable domain having the amino acid sequence of SEQ ID NO: 38.[000218] In some embodiments, according to the Kabat definition system, the anti- TMPRSS6 antibody of the present disclosure comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 1, a HC CDR2 having the amino acid sequence of SEQ ID NO: 2, a HC CDR3 having the amino acid sequence of SEQ ID NO: 35, a LC CDR1 having the amino acid sequence of SEQ ID NO: 36, a LC CDR2 having the amino acid sequence of RAN, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000219] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 1, HC CDR2 having the amino acid sequence of SEQ ID NO: 2, and HC CDR3 having the amino acid sequence of SEQ ID NO: 35. Alternatively or in addition, an anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2 or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 36, LC CDR2 having the amino acid sequence of RAN, and LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000220] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3 that collectively are at least 80% (e.g., 84#14616800v2at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 1, HC CDR2 having the amino acid sequence of SEQ ID NO: 2, and HC CDR3 having the amino acid sequence of SEQ ID NO: 35. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the to the LC CDR1 having the amino acid sequence of SEQ ID NO: 36, LC CDR2 having the amino acid sequence of RAN, and LC CDR3 having the amino acid sequence of SEQ ID NO: 6. [000221] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 1; a HC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR2 having the amino acid sequence of SEQ ID NO: 2; and / or a HC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR3 having the amino acid sequence of SEQ ID NO: 35. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 36; a LC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR2 having the amino acid sequence of RAN; and / or a LC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000222] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 1; a HC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR2 having the amino acid sequence SEQ ID NO: 2; and / or a HC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least85#14616800v297%, at least 98%, or at least 99%) identical to the HC CDR3 having the amino acid sequence of SEQ ID NO: 35. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR1 having the amino acid sequence of SEQ ID NO: 36; a LC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR2 having the amino acid sequence of RAN; and / or a LC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the LC CDR3 having the amino acid sequence of SEQ ID NO: 6.[000223] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising the amino acid sequence of SEQ ID NO: 37. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising the amino acid sequence of SEQ ID NO: 38.[000224] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19,18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH as set forth in SEQ ID NO: 37. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VL as set forth in SEQ ID NO: 38. In some embodiments, the number of amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a VH of SEQ ID NO: 37 and / or a VL of SEQ ID NO: 38 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20,19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of SEQ ID NO: 37, and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of SEQ ID NO: 38.86#14616800v2[000225] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the VH as set forth in SEQ ID NO: 37. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) to the VL as set forth in SEQ ID NO: 38. In some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a VH of SEQ ID NO: 37, and / or a VL of SEQ ID NO: 38 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibody provided herein comprise a heavy chain variable sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VH of SEQ ID NO: 37, and / or a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VL of SEQ ID NO: 38.[000226] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, HC CDR2 and HC CDR3 of a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 44. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, LC CDR2 and LC CDR3 of a light chain variable domain having the amino acid sequence of SEQ ID NO: 45.[000227] In some embodiments, according to the Kabat definition system, an anti- TMPRSS6 antibody of the present disclosure comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 13, a HC CDR2 having the amino acid sequence of SEQ ID NO: 43, a HC CDR3 having the amino acid sequence of SEQ ID NO: 15, a LC CDR1 having the amino acid sequence of SEQ ID NO: 16, a LC CDR2 having the amino acid sequence of WAF, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000228] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2, or 1 amino acid variation) as 87#14616800v2compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 13, HC CDR2 having the amino acid sequence of SEQ ID NO: 43, and HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, an anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2 or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 16, LC CDR2 having the amino acid sequence of WAF, and LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000229] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 13, HC CDR2 having the amino acid sequence of SEQ ID NO: 43, and HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the to the LC CDR1 having the amino acid sequence of SEQ ID NO: 16, LC CDR2 having the amino acid sequence of WAF, and LC CDR3 having the amino acid sequence of SEQ ID NO: 18. [000230] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 13; a HC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR2 having the amino acid sequence of SEQ ID NO: 43; and / or a HC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti- TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 16; a LC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR2 having the amino acid sequence of WAF; and / or a LC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid88#14616800v2variation) as compared with the LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000231] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 13; a HC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR2 having the amino acid sequence SEQ ID NO: 43; and / or a HC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR3 having the amino acid sequence of SEQ ID NO: 15. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR1 having the amino acid sequence of SEQ ID NO: 16; a LC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR2 having the amino acid sequence of WAF; and / or a LC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the LC CDR3 having the amino acid sequence of SEQ ID NO: 18.[000232] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising the amino acid sequence of SEQ ID NO: 44. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising the amino acid sequence of SEQ ID NO: 45.[000233] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH as set forth in SEQ ID NO: 44. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VL as set forth in SEQ ID NO: 45. In some 89#14616800v2embodiments, the number of amino acid variations e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a VH of SEQ ID NO: 44 and / or a VL of SEQ ID NO: 45 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of SEQ ID NO: 44, and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of SEQ ID NO: 45.[000234] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)to the VH as set forth in SEQ ID NO: 44. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the VL as set forth in SEQ ID NO: 45. In some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a VH of SEQ ID NO: 44, and / or a VL of SEQ ID NO: 45 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibody provided herein comprise a heavy chain variable sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VH of SEQ ID NO: 44, and / or a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VL of SEQ ID NO: 45.[000235] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, HC CDR2 and HC CDR3 of a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 49. Alternatively, or in addition, the anti-TMPRSS690#14616800v2antibody of the present disclosure comprises a LC CDR1, LC CDR2 and LC CDR3 of a light chain variable domain having the amino acid sequence of SEQ ID NO: 50.[000236] In some embodiments, according to the Kabat definition system, an anti- TMPRSS6 antibody of the present disclosure comprises a HC CDR1 having the amino acid sequence of SEQ ID NO: 24, a HC CDR2 having the amino acid sequence of SEQ ID NO: 48, a HC CDR3 having the amino acid sequence of SEQ ID NO: 26, a LC CDR1 having the amino acid sequence of SEQ ID NO: 27, a LC CDR2 having the amino acid sequence of WAT, and a LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000237] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence of SEQ ID NO: 24, HC CDR2 having the amino acid sequence of SEQ ID NO: 48, and HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3, which collectively contains no more than 5 amino acid variations (e.g., no more than 5, 4, 3, 2 or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 27, LC CDR2 having the amino acid sequence of WAT, and LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000238] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a HC CDR1, a HC CDR2, and a HC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)to the HC CDR1 having the amino acid sequence of SEQ ID NO: 24, HC CDR2 having the amino acid sequence of SEQ ID NO: 48, and HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a LC CDR1, a LC CDR2, and a LC CDR3 that collectively are at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the to the LC CDR1 having the amino acid sequence of SEQ ID NO: 27, LC CDR2 having the amino acid sequence of WAT, and LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000239] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR1 having the amino acid sequence 91#14616800v2of SEQ ID NO: 24; a HC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR2 having the amino acid sequence of SEQ ID NO: 48; and / or a HC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti- TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR1 having the amino acid sequence of SEQ ID NO: 27; a LC CDR2 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR2 having the amino acid sequence of WAT; and / or a LC CDR3 having no more than 3 amino acid variations (e.g., no more than 3, 2, or 1 amino acid variation) as compared with the LC CDR3 having the amino acid sequence of SEQ ID NO: 29.[000240] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises: a HC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR1 having the amino acid sequence of SEQ ID NO: 24; a HC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR2 having the amino acid sequence SEQ ID NO: 48; and / or a HC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the HC CDR3 having the amino acid sequence of SEQ ID NO: 26. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises: a LC CDR1 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR1 having the amino acid sequence of SEQ ID NO: 27; a LC CDR2 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) identical to the LC CDR2 having the amino acid sequence of WAT; and / or a LC CDR3 that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, , at least 98%, or at least 99%) identical to the LC CDR3 having the amino acid sequence of SEQ ID NO: 29.92#14616800v2[000241] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising the amino acid sequence of SEQ ID NO: 49. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising the amino acid sequence of SEQ ID NO: 50.[000242] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH containing no more than 20 amino acid variations (e.g., no more than 20, 19,18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VH as set forth in SEQ ID NO: 49. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the VL as set forth in SEQ ID NO: 50. In some embodiments, the number of amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) may occur within a VH of SEQ ID NO: 49 and / or a VL of SEQ ID NO: 50 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibodies provided herein comprise a heavy chain variable sequence that comprises a framework sequence that that contains no more than 20,19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VH of SEQ ID NO: 49, and / or a light chain variable sequence that comprises a framework sequence that that contains no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation to the framework sequence of a VL of SEQ ID NO: 50.[000243] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)%) identical to the VH as set forth in SEQ ID NO: 49. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a VL comprising an amino acid sequence that is at least 80% (e.g., at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%)identical to the VL as set forth in SEQ ID NO: 50. In some embodiments, the degree of sequence variation (e.g., at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%) may occur within a VH of SEQ ID NO: 49, and / or a VL of SEQ ID NO: 50 excluding any of the CDR sequences therein. In some embodiments, an anti-TMPRSS6 antibody provided herein 93#14616800v2comprise a heavy chain variable sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VH of SEQ ID NO: 49, and / or a light chain variable sequence that comprises a framework sequence that is at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the framework sequence of a VL of SEQ ID NO: 50.[000244] In some embodiments, an anti-TMPRSS6 antibody described herein is a chimeric antibody, which can include a heavy constant region and a light constant region from a human antibody. Chimeric antibodies refer to antibodies having a variable region or part of variable region from a first species and a constant region from a second species. Typically, in these chimeric antibodies, the variable region of both light and heavy chains mimics the variable regions of antibodies derived from one species of mammals (e.g, a non-human mammal such as mouse, rabbit, and rat), while the constant portions are homologous to the sequences in antibodies derived from another mammal such as human. In some embodiments, amino acid modifications can be made in the variable region and / or the constant region.[000245] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a VH domain and / or VL domain of any one of the anti-TMPRSS6 antibodies selected from Table 1, and comprises a constant region comprising the amino acid sequences of the constant regions of an IgG, IgE, IgM, IgD, IgA or IgY immunoglobulin molecule, any class (e.g., IgGl, IgG2, IgG3, IgG4, IgAl and IgA2), or any subclass (e.g, IgG2a and IgG2b) of immunoglobulin molecule. Non-limiting examples of human constant regions are described in the art, e.g., see Kabat E A et al., (1991) supra.[000246] In some embodiments, the light chain of any of the anti-TMPRSS6 antibodies described herein may further comprise a light chain constant region (CL), which can be any CL known in the art. In some examples, the CL is a kappa light chain. In other examples, the CL is a lambda light chain. In some embodiments, the CL is a kappa light chain.[000247] Other antibody heavy and light chain constant regions are well known in the art, e.g., those provided in the IMGT database (www.imgt.org) or at www.vbase2.org / vbstat.php., both of which are incorporated by reference herein.[000248] In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof, and a heavy chain constant region that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or 94#14616800v2at least 99% to SEQ ID NO: 9. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region that contains no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with SEQ ID NO: 9. In some embodiments, an anti- TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region set forth in SEQ ID NO: 9.[000249] In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 21. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region that contains no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with SEQ ID NO: 21. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region set forth in SEQ ID NO: 21.[000250] In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof, and a heavy chain constant region that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 39. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region that contains no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with SEQ ID NO: 39. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region set forth in SEQ ID NO: 39.[000251] In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof, and a 95#14616800v2heavy chain constant region that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 51. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region that contains no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with SEQ ID NO: 51. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising any one of the VH as listed in Table 1 or any variants thereof and a heavy chain constant region set forth in SEQ ID NO: 51.[000252] In some embodiments, an anti-TMPRSS6 antibody described herein comprises a light chain comprising any one of the VL as listed in Table 1 or any variants thereof, and a light chain constant region that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% to SEQ ID NO: 10. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a light chain comprising any one of the VL as listed in Table 1 or any variants thereof and a light chain constant region that contains no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with SEQ ID NO: 10. In some embodiments, an anti- TMPRSS6 antibody described herein comprises a light chain comprising any one of the VL as listed in Table 1 or any variants thereof and a light chain constant region set forth in SEQ ID NO: 10.[000253] In some embodiments, an anti-TMPRSS6 antibody described herein comprises a light chain comprising any one of the VL as listed in Table 1 or any variants thereof, and a light chain constant region that is at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% to SEQ ID NO: 40. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a light chain comprising any one of the VL as listed in Table 1 or any variants thereof and a light chain constant region that contains no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with SEQ ID NO: 40. In some embodiments, an anti- TMPRSS6 antibody described herein comprises a light chain comprising any one of the VL as listed in Table 1 or any variants thereof and a light chain constant region set forth in SEQ96#14616800v2ID NO: 40. Examples of IgG heavy chain and light chain amino acid sequences of the anti- TMPRSS6 antibodies described are provided in Table 1 above.[000254] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a heavy chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the heavy chain as set forth in SEQ ID NO: 11. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a light chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the light chain as set forth in SEQ ID NO: 12. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising an amino acid sequence that is at least 80% at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% to SEQ ID NO: 11. Alternatively or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising an amino acid sequence that is at least 80% at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 12. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 11. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising the amino acid sequence of SEQ ID NO: 12.[000255] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a heavy chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the heavy chain as set forth in SEQ ID NOs: 17 or 22. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a light chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the light chain as set forth in SEQ ID NO: 23. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NOs: 17 or 22. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising an amino acid sequence that is at least80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical97#14616800v2to SEQ ID NO: 23. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising the amino acid sequence of SEQ ID NOs: 17 or 22. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising the amino acid sequence of SEQ ID NO: 23.[000256] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a heavy chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the heavy chain as set forth in SEQ ID NO: 33. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a light chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the light chain as set forth in SEQ ID NO: 34. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 33. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 34. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 33. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising the amino acid sequence of SEQ ID NO: 34.[000257] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a heavy chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the heavy chain as set forth in SEQ ID NO: 41. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a light chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the light chain as set forth in SEQ ID NO: 42. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 41. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 42. In some 98#14616800v2embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 41. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising the amino acid sequence of SEQ ID NO: 42.[000258] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a heavy chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the heavy chain as set forth in SEQ ID NO: 46. Alternatively, or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a light chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the light chain as set forth in SEQ ID NO: 47. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 46. Alternatively, or in addition, an anti-TMPRSS6 antibody described herein comprises a light chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 47. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 46. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising the amino acid sequence of SEQ ID NO: 47.[000259] In some embodiments, an anti-TMPRSS6 antibody of the present disclosure comprises a heavy chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the heavy chain as set forth in SEQ ID NO: 52. Alternatively or in addition, the anti-TMPRSS6 antibody of the present disclosure comprises a light chain containing no more than 20 amino acid variations (e.g., no more than 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid variation) as compared with the light chain as set forth in SEQ ID NO: 53. In some embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 52. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising an amino acid sequence that is at least 80% (e.g., 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99%) identical to SEQ ID NO: 53. In some 99#14616800v2embodiments, an anti-TMPRSS6 antibody described herein comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 52. Alternatively, or in addition, the anti-TMPRSS6 antibody described herein comprises a light chain comprising the amino acid sequence of SEQ ID NO: 53.[000260] The anti-TMPRSS6 antibodies described herein can be in any antibody form, including, but not limited to, intact (i.e., full-length) antibodies, antigen-binding fragments thereof (such as Fab, Fab', F(ab)2, Fv), single chain antibodies, bi-specific antibodies, or nanobodies. In some embodiments, an anti-TMPRSS6 antibody described herein is a scFv. In some embodiments, an anti-TMPRSS6 antibody described herein is a scFv-Fab (e.g., scFv fused to a portion of a constant region).[000261] In some embodiments, conservative mutations can be introduced into antibody sequences (e.g., CDRs or framework sequences) at positions where the residues are not likely to be involved in interacting with a target antigen (e.g., TMPRSS6), for example, as determined based on a crystal structure. In some embodiments, one, two or more mutations (e.g., amino acid substitutions) are introduced into the Fc region of an anti-TMPRSS6 antibody described herein (e.g., in a CH2 domain (residues 231-340 of human IgGl) and / or CH3 domain (residues 341-447 of human IgGl) and / or the hinge region, with numbering according to the Kabat numbering system (e.g, the EU index in Kabat)) to alter one or more functional properties of the antibody, such as serum half-life, complement fixation, Fc receptor binding and / or antigen-dependent cellular cytotoxicity.[000262] In some embodiments, one, two or more mutations (e.g, amino acid substitutions) are introduced into the hinge region of the Fc region (CHI domain) such that the number of cysteine residues in the hinge region are altered (e.g., increased or decreased) as described in, e.g., U.S. Pat. No. 5,677,425. The number of cysteine residues in the hinge region of the CHI domain can be altered to, e.g., facilitate assembly of the light and heavy chains, or to alter (e.g., increase or decrease) the stability of the antibody or to facilitate linker conjugation.[000263] In some embodiments, one, two or more mutations (e.g., amino acid substitutions) are introduced into the Fc region of an antibody described herein (e.g., in a CH2 domain (residues 231-340 of human IgGl) and / or CH3 domain (residues 341-447 of human IgGl) and / or the hinge region, with numbering according to the Kabat numbering system (e.g., the EU index in Kabat)) to increase or decrease the affinity of the antibody for an Fc receptor (e.g., an activated Fc receptor) on the surface of an effector cell. Mutations in the Fc region of an antibody that decrease or increase the affinity of an antibody for an Fc receptor and techniques for introducing such mutations into the Fc receptor or fragment thereof are known100#14616800v2to one of skill in the art. Examples of mutations in the Fc receptor of an antibody that can be made to alter the affinity of the antibody for an Fc receptor are described in, e.g., Smith P et al., (2012) PNAS 109: 6181-6186, U.S. Pat. No. 6,737,056, and International Publication No.; WO 97 / 34631, which are incorporated herein by reference.[000264] In some embodiments, one, two or more amino acid mutations (i.e., substitutions, insertions or deletions) are introduced into an IgG constant domain, or FcRn-binding fragment thereof (preferably an Fc or hinge-Fc domain fragment) to alter (e.g., decrease or increase) half-life of the antibody in vivo. See, e.g., International Publication Nos. WO 97 / 34631; and U.S. Pat. Nos. 5,869,046, 6,121,022, 6,277,375 and 6,165,745 for examples of mutations that will alter (e.g., decrease or increase) the half-life of an antibody in vivo.[000265] In some embodiments, one, two or more amino acid mutations (i.e., substitutions, insertions, or deletions) are introduced into an IgG constant domain, or FcRn-binding fragment thereof (preferably an Fc or hinge-Fc domain fragment) to decrease the half-life of the anti-TMPRSS6 antibody in vivo. In some embodiments, one, two or more amino acid mutations (i.e., substitutions, insertions, or deletions) are introduced into an IgG constant domain, or FcRn-binding fragment thereof (preferably an Fc or hinge-Fc domain fragment) to increase the half-life of the antibody in vivo. In some embodiments, the antibodies can have one or more amino acid mutations (e.g., substitutions) in the second constant (CH2) domain (residues 231-340 of human IgGl) and / or the third constant (CH3) domain (residues 341-447 of human IgGl), with numbering according to the EU index in Kabat (Kabat E A et al., (1991) supra). In some embodiments, the constant region of the IgGl of an antibody described herein comprises a methionine (M) to tyrosine (Y) substitution in position 252, a serine (S) to threonine (T) substitution in position 254, and a threonine (T) to glutamic acid (E) substitution in position 256, numbered according to the EU index as in Kabat. See U.S. Pat. No. 7,658,921, which is incorporated herein by reference. This type of mutant IgG, referred to as " YTE mutant" has been shown to display four-fold increased half-life as compared to wild-type versions of the same antibody (see Dall'Acqua W F et al., (2006) J Biol Chem 281 : 23514-24).[000266] In some embodiments, one, two or more amino acid substitutions are introduced into an IgG constant domain Fc region to alter the effector function(s) of the anti-TMPRSS6 antibody. The effector ligand to which affinity is altered can be, for example, an Fc receptor or the Cl component of complement. This approach is described in further detail in U.S. Pat. Nos. 5,624,821 and 5,648,260. In some embodiments, one or more amino acid substitutions may be introduced into the Fc region of an antibody described herein to remove potential 101#14616800v2glycosylation sites on Fc region, which may reduce Fc receptor binding (see, e.g., Shields R L et al., (2001) J Biol Chem 276: 6591-604).[000267] In some embodiments, one or more amino in the constant region of an anti- TMPRSS6 antibody described herein can be replaced with a different amino acid residue such that the antibody has altered Clq binding and / or reduced or abolished complement dependent cytotoxicity (CDC). This approach is described in further detail in U.S. Pat. No. 6,194,551 (Idusogie et al). In some embodiments, one or more amino acid residues in the N- terminal region of the CH2 domain of an antibody described herein are altered to thereby alter the ability of the antibody to fix complement. This approach is described further in International Publication No. WO 94 / 29351. In some embodiments, the Fc region of an antibody described herein is modified to increase the ability of the antibody to mediate antibody dependent cellular cytotoxicity (ADCC) and / or to increase the affinity of the antibody for an Fey receptor. This approach is described further in International Publication No. WO 00 / 42072.[000268] In some embodiments, the heavy and / or light chain variable domain(s) sequence(s) of the antibodies provided herein can be used to generate, for example, CDR-grafted, chimeric, humanized, or composite human antibodies or antigen-binding fragments, as described elsewhere herein. As understood by one of ordinary skill in the art, any variant, CDR-grafted, chimeric, humanized, or composite antibodies derived from any of the antibodies provided herein may be useful in the compositions and methods described herein and will maintain the ability to specifically bind TMPRSS6, such that the variant, CDR- grafted, chimeric, humanized, or composite antibody has at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95% or more binding to TMPRSS6 relative to the original antibody from which it is derived.[000269] In some embodiments, the antibodies provided herein comprise mutations that confer desirable properties to the antibodies. For example, to avoid potential complications due to Fab-arm exchange, which is known to occur with native IgG4 mAbs, the antibodies provided herein may comprise a stabilizing ‘Adair’ mutation (Angal S., et al., A single amino acid substitution abolishes the heterogeneity of chimeric mouse / human (IgG4) antibody, Mol Immunol 30, 105-108; 1993), where serine 228 (EU numbering; residue 241 Kabat numbering) is converted to proline resulting in an IgGl-like hinge sequence. Accordingly, any of the antibodies may include a stabilizing ‘Adair’ mutation.[000270] In some embodiments, an antibody is modified, e.g., modified via glycosylation, phosphorylation, sumoylation, and / or methylation. In some embodiments, an antibody is a 102#14616800v2glycosylated antibody, which is conjugated to one or more sugar or carbohydrate molecules. In some embodiments, the one or more sugar or carbohydrate molecule are conjugated to the antibody via N-glycosylation, O-glycosylation, C-glycosylation, glypiation (GPI anchor attachment), and / or phosphoglycosylation. In some embodiments, the one or more sugar or carbohydrate molecules are monosaccharides, di saccharides, oligosaccharides, or glycans. In some embodiments, the one or more sugar or carbohydrate molecule is a branched oligosaccharide or a branched glycan. In some embodiments, the one or more sugar or carbohydrate molecule includes a mannose unit, a glucose unit, an N-acetylglucosamine unit, an N-acetylgalactosamine unit, a galactose unit, a fucose unit, or a phospholipid unit. In some embodiments, there are about 1-10, about 1-5, about 5-10, about 1-4, about 1-3, or about 2 sugar molecules. In some embodiments, a glycosylated antibody is fully or partially glycosylated. In some embodiments, an antibody is glycosylated by chemical reactions or by enzymatic means. In some embodiments, an antibody is glycosylated in vitro or inside a cell, which may optionally be deficient in an enzyme in the N- or O- glycosylation pathway, e.g. a glycosyltransferase. In some embodiments, an antibody is functionalized with sugar or carbohydrate molecules as described in International Patent Application Publication WO2014065661, published on May 1, 2014, entitled, “Modified antibody, antibodyconjugate and process for the preparation thereof .[000271] In some embodiments, any one of the anti-TMPRSS6 antibodies described herein may comprise a signal peptide in the heavy and / or light chain sequence (e.g., a N-terminal signal peptide). In some embodiments, the anti-TMPRSS6 antibody described herein comprises any one of the VH and VL sequences, or any one of the IgG heavy chain and light chain sequences described herein, and further comprises a signal peptide e.g., a N-terminal signal peptide).IV. Kits for Therapeutic and Diagnostic Applications[000272] The present disclosure also provides kits for the therapeutic or diagnostic applications as disclosed herein. Such kits can include one or more containers comprising an antibody composition, e.g., any of those described herein.[000273] In some embodiments, the kit can comprise instructions for use in accordance with any of the methods described herein. The included instructions can comprise a description of administration of the antibody composition (e.g., comprising anti-TMPRSS6 antibody) to treat a target disease (e.g., as those described herein). The kit may further comprise a description of selecting an individual suitable for treatment based on identifying whether that103#14616800v2individual has the target disease. In still other embodiments, the instructions comprise a description of administering an antibody composition (e.g., comprising anti-TMPRSS6 antibody) to an individual at risk of the target disease.[000274] The instructions relating to the use of an antibody composition (e.g., comprising anti-TMPRSS6 antibody) generally include information as to dosage, dosing schedule, and route of administration for the intended treatment. The containers may be unit doses, bulk packages (e.g., multi-dose packages) or sub-unit doses. Instructions supplied in the kits of the invention are typically written instructions on a label or package insert (e.g., a paper sheet included in the kit), but machine-readable instructions (e.g., instructions carried on a magnetic or optical storage disk) are also acceptable.[000275] The label or package insert indicates that the composition is used for treating, delaying the onset and / or alleviating a disease or disorder. Instructions may be provided for practicing any of the methods described herein.[000276] The kits of this invention are in suitable packaging. Suitable packaging includes, but is not limited to, vials, bottles, jars, flexible packaging (e.g., sealed Mylar or plastic bags), and the like.[000277] Also contemplated are packages for use in combination with a specific device, such as an infusion device, such as a minipump. A kit may have a sterile access port (for example the container may be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). The container may also have a sterile access port (for example the container may be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). At least one active agent in the composition is an anti-TMPRSS6 antibody as those described herein.[000278] Kits may optionally provide additional components such as buffers and interpretive information. Normally, the kit comprises a container and a label or package insert(s) on or associated with the container. In some embodiments, the invention provides articles of manufacture comprising contents of the kits described above.[000279] Also provided herein are kits for use in detecting TMPRSS6 in a sample. Such a kit may comprise any of the antibody compositions (e.g., comprising anti-TMPRSS6 antibodies) described herein. In some embodiments, an anti-TMPRSS6 antibody formulated in a composition as described herein can be conjugated with a detectable label. As used herein, “conjugated” or “attached” means two entities are associated, preferably with sufficient affinity that the therapeutic / diagnostic benefit of the association between the two entities is realized. The association between the two entities can be either direct or via a 104#14616800v2linker, such as a polymer linker. Conjugated or attached can include covalent or noncovalent bonding as well as other forms of association, such as entrapment, e.g., of one entity on or within the other, or of either or both entities on or within a third entity, such as a micelle. [000280] Alternatively, or in addition, the kit may comprise a secondary antibody capable of binding to anti-TMPRSS6 antibody. The kit may further comprise instructions for using the antibody composition (e.g., comprising anti-TMPRSS6 antibody) for detecting TMPRSS6.[000281] In order that the invention described herein may be more fully understood, the following examples are set forth. The examples described in this application are offered to illustrate the compositions, methods, devices, and systems provided herein and are not to be construed in any way as limiting their scope.EXAMPLESExample 1: Development of a Stress-Resistant Antibody Formulation[000282] Development of a formulation comprising an anti-TMPRSS6 antibody was carried out to create an antibody formulation with the following characteristics: (a) a liquid antibody formulation sufficient to deliver a dose of 100 mg or more of antibody via subcutaneous injection; (b) a formulation compatible with and stable in a Type 1 clear glass vial and standard serum stopper packaging; and (c) a sterile drug product solution that supports longterm stability. As used in this experiment, characteristics of long-term stability comprised: (1) minimizing formation of high molecular weight species when subjected to handling and thermal and light stresses; (2) minimizing changes in the relative distribution of charged species when subjected to thermal and light stresses; and (3) minimizing changes to appearance when subjected to thermal and light stresses. The anti-TMPRSS6 antibody used in all experiments was an anti-TMPRSS6 antibody having a heavy chain comprising the amino acid sequence of SEQ ID NO: 52 and a light chain comprising the amino acid sequence of SEQ ID NO: 53. Four primary protein stress conditions were used throughout formulation development to represent extreme handling conditions beyond which the drug product would not be subjected to during handling, manufacturing, shipping, storing, and labeling. These stress conditions were employed to develop the antibody formulations and to evaluate the effects of potential real-world stresses on the stability of the drug product. The stress conditions tested were as follows:105#14616800v2(1) subjecting the protein (i.e., anti-TMPRSS6 antibody) to multiple freeze-thaw cycles. Because the protein must undergo at least one freeze-thaw cycle during the manufacturing process, multiple freeze-thaw cycles were carried out that would exceed the actual stress that the protein would be expected to experience;(2) incubating the antibody solution at elevated temperature (40°C) relative to the proposed drug product storage condition (e.g., 2-8°C);(3) agitation of the antibody solution at elevated temperature. The agitation stress tested was continuous agitation in glass vials that exceeds the agitation expected to occur during the handling and manufacturing process; and(4) exposing the protein (i.e., anti-TMPRSS6 antibody) to 1.2 million lux hours of visible light and 200 W-h / m2of UV light. The light exposure conditions tested were significantly harsher than the light stress expected to occur during handling, manufacturing, shipping, storing, and labeling of the drug product.[000283] The goals for the development of the stress-resistant antibody formulation included the selection of the buffer concentration and the identification of stabilizing excipients. Buffer concentration can significantly affect the stability and viscosity of proteins in a liquid solution. Furthermore, the addition of amino acids was examined for their ability to improve the stability of the drug product (e.g., a stress-sensitive antibody).[000284] Initial formulation studies were conducted using 50-200 mg / mL of anti-TMPRSS6 antibody and carried out with screening buffers, cosolvents, thermal and light stabilizers, and viscosity reducers. Following the results from these initial studies, a second phase of formulation studies were conducted using 175 mg / mL of anti-TMPRSS6 antibody to test the effect of buffer concentration and the introduction of a photo-stabilizer to enhance protein stability. Throughout development, the formulations were assessed for stress and storage stability.[000285] Results generated from these studies were used to develop a stable liquid formulation suitable for clinical use (e.g., for subcutaneous administration). The formulations that were developed met the one or more of the following non-limiting objectives defined for formulation development: (1) suitable for subcutaneous administration; (2) tonicity not exceeding maximum allowable tonicity for subcutaneous administration; and (3) the sterile drug product solution demonstrating improvements in thermal- and photo-stability compared to a control formulation. Improved thermal- and photo-stability were assessed in these experiments through: (a) minimal formation of degradation of high molecular weight species; (b) fewer changes in relative distribution of charged species; (c) minimal changes in106#14616800v2subvisible particles; and (d) improvement in appearance after exposure to thermal and light stress compared to control.Example 2. Exemplary Stress-Resistant Formulations[000286] Using the methods described herein, pharmaceutical formulations were developed exhibiting high stability, low viscosity, and isotonic-to-hypertonic tonicity. These formulations comprised: (i) a human antibody that specifically binds to human TMPRSS6 (anti-hTMPRSS6) having a heavy chain comprising the amino acid sequence of SEQ ID NO: 52 and a light chain comprising the amino acid sequence of SEQ ID NO: 53 at a concentration of 175 mg / mL; (ii) a histidine buffer system that provides sufficient buffering at a pH of 5.6 ± 0.3; (iii) an organic surfactant that protects the structural integrity of the antibody (e.g., polysorbate 80); (iv) a sugar thermal stabilizer (e.g., sucrose); (v) an amino acid viscosity modifier (e.g., histidine and arginine); and optionally (vi) an amino acid photoprotectant (e.g., methionine and histidine). Five illustrative formulations of formulations with these desired characteristics include:[000287] Formulation 1 : (i) 175 mg / mL anti-TMPRSS6 antibody; (ii) 20 mM histidine (L- histidine monohydrochloride; L-His-HCl) buffer that buffers at pH = 5.6 ± 0.3; (iii) 0.2mg / mL polysorbate 80; (iv) 20mg / mL sucrose; (v) 100 mM arginine (L-Arginine monohydrochloride; L-Arg-HCl).[000288] Formulation 2: (i) 175 mg / mL anti-TMPRSS6 antibody; (ii) 50 mM histidine (L- His-HCl) buffer that buffers at pH = 5.6 ± 0.3; (iii) 0.2mg / mL polysorbate 80; (iv) 20mg / mL sucrose; and (v) 100 mM arginine (L-Arg-HCl).[000289] Formulation 3: (i) 175 mg / mL anti-TMPRSS6 antibody; (ii) 100 mM histidine (L- His-HCl) buffer that buffers at pH = 5.6 ± 0.3; (iii) 0.2mg / mL polysorbate 80; (iv) 20mg / mL sucrose; and (v) 100 mM arginine (L-Arg-HCl).[000290] Formulation 4: (i) 175 mg / mL anti-TMPRSS6 antibody; (ii) 20 mM histidine (L- His-HCl) buffer that buffers at pH = 5.6 ± 0.3; (iii) 0.2mg / mL polysorbate 80; (iv) 20mg / mL sucrose; (v) 100 mM arginine (L-Arg-HCl); and (vi) 10 mM methionine (L-Methionine monohydrochloride; L-Met-HCl).[000291] Formulation 5: (i) 175 mg / mL anti-TMPRSS6 antibody; (ii) 50 mM histidine (L- His-HCl) buffer that buffers at pH 5.6 + / - 0.3; (iii) 0.2mg / mL polysorbate 80; (iv) 20mg / mL sucrose; (v) lOOmM arginine (L-Arg-HCl); and (vi) lOmM methionine (L-Met-HCl).107#14616800v2Example 3. Effect of Freeze-Thaw Cycles in Formulations with Different Buffers[000292] Formulations comprising the buffer systems indicated in Table 3 were subjected to three freeze-thaw cycles where each vial containing the indicated formulation was frozen at - 70°C, then brought to ambient room temperature (~25°C). Each vial remained frozen overnight, then brought to room temperature and allowed to thaw for no less than 30 minutes and no more than 1 hour. Once the formulations were determined to be completed thawed (as assessed visually by lack of ice granules), the samples were placed back into the freezer to begin the next cycle. The samples were subjected to three total freeze-thaw cycles. The results of these experiments are shown in Table 3 below. It was observed that freeze-thaw cycles had no effect on the stability of the protein regardless of differences in histidine or methionine concentration.Table 3: Effect of histidine concentration and the addition of methionine on the stability of 175 mg / mL protein after three freeze-thaw cycles.Abbreviations: FP = free of particles; HMW = high molecular weight species, main = native antibody; LMW = low molecular weight species; SEC = size exclusion chromatography; CEX = cation exchange chromatography; CE-SDS = capillary electrophoresis sodium dodecyl sulfate; HC = heavy chain; LC = light chain; NGHC = nonglycosylated heavy chain; PS80 = polysorbate 80.Example 4. Effect of Thermal Stress in Formulations with Different Buffers[000293] The effect of buffer concentration on the thermal stability of antibodies was examined by incubating solutions comprising 175 mg / mL anti-TMPRSS6 antibody at 40°C for 28 days in a series of different histidine concentrations (indicated in Table 4).Formulations comprising the following concentrations of histidine were studied: 20 mM, 50 108#14616800v2mM, and 100 mM. Additionally, the addition of methionine was evaluated for its potential improvement on protein stability. 10 mM methionine was added to the base formulation with either 20 mM or 50 mM histidine. Table 4 shows the effect of the buffer concentration on protein stability when the protein was incubated at 40°C for 28 days.[000294] These results demonstrated that increasing histidine concentrations in formulations provided an improvement in formulation appearance, as evidenced by less turbidity and no particulate formation (i.e., increased stability), after incubation at 40°C for 28 days compared to the formulations with lower histidine concentrations (see, e.g., clarity of 20 mM histidine versus 100 mM histidine). Furthermore, formulations with the addition of methionine showed no change in color after incubation at 40°C for 28 days, while the other formulations showed a slightly darker solution, indicating a stabilizing effect with the addition of methionine. There was also an improvement in charged variant formation when using either (a) 100 mM histidine, or (b) 50 mM histidine + 10 mM methionine.Table 4: Effect of histidine concentration on the stability of 175 mg / mL protein incubated at 40°C for 28 days.Abbreviations: NEFP = not essentially free of particles; FP = free of particles; HMW = high molecular weight species, LMW = low molecular weight species; SEC = size exclusion chromatography; CEX = cation exchange chromatography; CE-SDS = capillary electrophoresis sodium dodecyl sulfate; HC = heavy chain; LC = light chain; NGHC = non-glycosylated heavy chain; PS80 = polysorbate 80.#14616800v2Example 5. Effect of Thermal Stress with Agitation in Formulations with Different Buffers[000295] The effect of buffer concentration on the thermal stability of protein in the presence of physical agitation was examined. Vials filled with the formulations indicated in Table 5 and comprising 175 mg / mL anti-TMPRSS6 antibody were incubated at 40°C for 3 days with constant rotation of 300 rpm, then remained stationary for 11 days at 40°C prior to evaluation. The results of these experiments are shown in Table 5 below. It was observed that the effect of agitation in combination with thermal stress was minimal for all formulations tested, and the degree of degradation was comparable for each formulation.Table 5: Effect of buffer concentration on the stability of 175 mg / mL protein subjected to thermal stress with agitation.Abbreviations: NEFP = not essentially free of particles; FP = free of particles; HMW = high molecular weight species, LMW = low molecular weight species; SEC = size exclusion chromatography; CEX = cation exchange chromatography; CE-SDS = capillary electrophoresis sodium dodecyl sulfate; HC = heavy chain; LC = light chain; NGHC = non-glycosylated heavy chain; PS80 = polysorbate 80.Example 6. Effect of Light Stress in Formulations with Different Buffers110#14616800v2[000296] The effect of buffer concentration on the light stability of protein was examined. Vials filled with the formulations indicated in Table 6 were placed in a light box, where they were subjected to 5000 lux for 10 days at 25°C, followed by 50 hours of UV exposure at 4 W / m2. Table 6 summarizes the change in stability of the anti-TMPRSS6 antibody for each formulation after exposure to light stress.[000297] The results demonstrated that when the formulations were subjected to light stress, significant protein degradation was observed, but increasing the concentration of histidine in the formulation reduced production of charged variants compared to the formulations with less histidine (see, e.g., Table 6, 100 mM histidine versus 20 mM histidine). Furthermore, the addition of methionine showed an improvement on color and clarity compared to formulations without methionine.Table 6: Effect of buffer concentration on the stability of 175 mg / mL protein subjected to light stress.Abbreviations: NEFP = not essentially free of particles; FP = free of particles; HMW = high molecular weight species, LMW = low molecular weight species; SEC = size exclusion chromatography; CEX = cation exchange chromatography; CE-SDS = capillary electrophoresis sodium dodecyl sulfate; HC = heavy chain; LC = light chain; NGHC = non-glycosylated heavy chain; PS80 = polysorbate 80.Example 7. Peptide Map Analysis on Proteins in Stressed Formulations111#14616800v2[000298] Formulations comprising 175 mg / mL anti-TMPRSS6 antibodies and different buffer concentrations as indicated in Table 7 were subjected to peptide mapping to determine the degree of post-translational modifications (PTMs) after exposure to thermal and light stresses. Each sample was denatured with guanidine-hydrochloride in Tris-HCl buffer, reduced by dithiothreitol (DTT), and cysteine-alkylated with iodoacetamide (IAM).Following sample clean-up, the protein was digested with Lys-C / trypsin sequential digestion to obtain peptides suitable for subsequent analysis. Table 7 below lists the samples that underwent peptide mapping analysis.Table 7. Formulations Comprising 175 mg / mL anti-TMPRSS6 Antibody Subjected to Peptide Mapping[000299] N-terminal glutamine modified as pyro-glutamic acid was reported with higher ratios in all stressed samples compared to non-stressed conditions. In addition, modifications such as methionine oxidation and di-oxidation, tryptophan oxidation and di-oxidation, tryptophan-C6H5N di-oxidation, isomerization, histidine di-oxidation, histidine-HCN di- oxidation, lysine glycation, asparagine deamidation, and succinimide formation were observed.[000300] The measured masses of the peptides were compared to the theoretical masses to verify the correct identification of each peptide, and the mutation or PTM sites were determined and manually confirmed. The PTM ratio was semi-quantitated by extracted ion chromatograms (EICs) using the following equation:112#14616800v2[000301] The oxidation ratio was significantly increased in light stressed samples (Samples la-3a) compared to samples that underwent thermal stress (Samples lb-3b). The presence of methionine oxidation and di-oxidation, histidine di-oxidation, and histidine di-oxidation-HCL in the 20 mM histidine sample was significantly higher compared to other light stressed samples (see Sample la versus Samples 2a and 3a).[000302] Thermal (40°C) stress induced significantly higher ratios of asparagine deamidation on the 326N residue of the heavy chain of the anti-TMPRSS6 antibody. A higher ratio of lysine glycation was detected in the 20 mM histidine and 50 mM histidine + 10 mM methionine samples (Samples lb and 3b) compared to the samples with 100 mM histidine (Sample 2b). The ratios of oxidation and isomerization were comparable among all samples subjected to thermal stress. The ratios of other PTMs were likewise found to be comparable among all samples subjected to thermal stress.[000303] While methionine was chosen for its potential ability to protect the protein from light stress-induced oxidation, surprisingly, the peptide map data indicated that higher concentrations of histidine were also effective as a light protectant. Tables 8 and 9 show the ratio results of each PTM and glycation site for peptides from all formulations.Table 8. PTM Results113#14616800v2The first row of each group depicts the unmodified peptide (used to calculate the EIC ratio). pE(Q) = N-terminal glutamine modified as pyro-glutamic acid.IsomerizationA= modification sites that cannot be identified by current MS / MS data (e.g., species have the same molecular weight but elute at 2 different retention times; site of isomerization unclear).WiIdcard(97.0491)* = this species may coincide with 6*Oxidation component detected in the reduced mass, but the specific modification is unclear.Table 9. Glycation ResultsThe first row of each group depicts the unmodified peptide (used to calculate the EIC ratio).Glycation(K)* = the EIC ratio for glycation at this site was overestimated, as one of the unmodified peptides was unidentified due to poor retention.114#14616800v2

Claims

1. CLAIMSWhat is claimed:

1. A composition comprising a stress-sensitive antibody formulated with histidine and optionally methionine in amounts effective to promote resistance of the antibody to light stress and / or thermal stress.

2. The composition of claim 1, wherein histidine and the antibody are present in the composition in a molar ratio of 12: 1-150: 1 histidine: antibody.

3. The composition of claim 1 or 2, wherein methionine and the antibody are present in the composition in a molar ratio of 0: 1-20: 1 methionine:antibody.

4. The composition of any one of claims 1-3, wherein the composition is a solution.

5. The composition of any one of claims 1-4, wherein the composition comprises the antibody at a concentration of 120-500 mg / mL.

6. The composition of any one of claims 1-5, wherein the composition comprises histidine at a concentration of 45-150 mM.

7. The composition of any one of claims 1-6, wherein the composition comprises histidine at a concentration of 50-100 mM.

8. The composition of any one of claims 1-7, wherein the composition comprises histidine at a concentration of 50 mM.

9. The composition of any one of claims 1-7, wherein the composition comprises histidine at a concentration of 100 mM.

10. The composition of any one of claims 1-9, wherein the histidine is L-histidine (L- His), D-histidine, or any salt thereof.115#14616800v211. The composition of any one of claims 1-10, wherein the histidine is histidine monohydrochloride (His-HCl), histidine sulfate, or histidine acetate, optionally wherein the histidine is L-His monohydrochloride (L-His-HCl).

12. The composition of any one of claims 1-11, wherein the composition comprises methionine at a concentration of 0-20 mM.

13. The composition of any one of claims 1-12, wherein the composition comprises methionine at a concentration of 10 mM.

14. The composition of any one of claims 1-13, wherein the methionine is L-methionine, D-methionine, or any salt thereof, optionally wherein the methionine is L-methionine monohydrochloride.

15. The composition of any one of claims 1-14, wherein the composition comprises the antibody at a concentration of 175 mg / mL.

16. The composition of any one of claims 1-14, wherein the composition comprises the antibody at a concentration of 150 mg / mL.

17. The composition of any one of claims 1-16, wherein the composition further comprises arginine.

18. The composition of claim 17, wherein the composition comprises arginine at a concentration of 10-500 mM.

19. The composition of claim 17 or 18, wherein the composition comprises arginine at a concentration of 50-200 mM.

20. The composition of any one of claims 17-19, wherein the composition comprises arginine at a concentration of 100 mM.

21. The composition of any one of claims 1-20, wherein the composition further comprises a sugar.116#14616800v222. The composition of claim 21, wherein the sugar is sucrose, maltose, or trehalose.

23. The composition of claim 21 or 22, wherein the sugar is sucrose.

24. The composition of claim 23, wherein the composition comprises lOmg / mL to 50mg / mL of sucrose.

25. The composition of any one of claims 1-24, wherein the composition further comprises a surfactant.

26. The composition of claim 25, wherein the surfactant is sodium dodecyl sulfate (SDS), polysorbate, or a nonionic surfactant.

27. The composition of claim 25 or 26, wherein the surfactant is polysorbate 20 or polysorbate 80.

28. The composition of claim 27, wherein the composition comprises 0.05mg / mL to 0.5mg / mL of polysorbate.

29. The composition of any one of claims 1-28, wherein the composition has a pH of 5-7.

30. The composition of any one of claims 1-29, wherein the composition has a pH of 5.6.

31. The composition of any one of claims 1-30, wherein the composition is lyophilized.

32. The composition of any one of claims 1-31, wherein the antibody is stable in the composition at 40°C for at least two weeks.

33. The composition of any one of claims 1-32, wherein the antibody is stable when the composition is exposed to at least 1.2 million lux hours.

34. The composition of any one of claims 1-33, wherein the antibody is stable when the composition is exposed to at least 200 W-h / m2of UV light.117#14616800v235. The composition of any one of claims 1-34, wherein the antibody is stable after being agitated at a speed of 100-1000 rpm at 40°C for at least 3 days.

36. The composition of claim 35, wherein the antibody is stable after the composition is stored at 40°C for at least 10 days after agitation.

37. The composition of any one of claims 1-36, wherein the antibody in the composition retains purity of at least 93% after being subjected to 40°C for at least two weeks, exposed to light at an illuminance of at least 1.2 million lux hours, exposed to at least 200 W-h / m2of UV light, agitated at a speed of 100-1000 rpm at 40°C for at least 3 days, or any combination thereof.

38. The composition of any one of claims 1-37, wherein the composition comprises less than 7% high molecular weight aggregates after being subjected to 40°C for at least two weeks, exposed to light at an illuminance of at least 1.2 million lux hours, exposed to at least 200 W-h / m2of UV light, agitated at a speed of 100-1000 rpm at 40°C for at least 3 days, or any combination thereof.

39. The composition of any one of claims 1-38, wherein the composition comprises less than 0.7% low molecular weight impurities after being subjected to 40°C for at least two weeks, exposed to light at an illuminance of at least 1.2 million lux hours, exposed to at least 200 W-h / m2of UV light, agitated at a speed of 100-1000 rpm at 40°C for at least 3 days, or any combination thereof.

40. The composition of any one of claims 1-39, wherein the composition comprises less than 7000 counts / mL sub-visible particles that are at least 2 pm in size after being subjected to 40°C for at least two weeks, exposed to light at an illuminance of at least 1.2 million lux hours, exposed to at least 200 W-h / m2of UV light, agitated at a speed of 100-1000 rpm at 40°C for at least 3 days, or any combination thereof.

41. The composition of any one of claims 1-40, wherein the composition comprises less than 500 counts / mL sub-visible particles that are at least 5 pm in size after being subjected to 40°C for at least two weeks, exposed to light at an illuminance of at least 1.2 million lux118#14616800v2hours, exposed to at least 200 W-h / m2of UV light, agitated at a speed in the range of 100- 1000 rpm at 40°C for at least 3 days, or any combination thereof.

42. The composition of any one of claims 1-41, wherein the composition has a viscosity of less than 15 mPa-s after being subjected to 40°C for at least two weeks, exposed to light at an illuminance of at least 1.2 million lux hours, exposed to at least 200 W-h / m2of UV light, agitated at a speed in the range of 100-1000 rpm at 40°C for at least 3 days, or any combination thereof.

43. The composition of any one of claims 1-42, wherein the composition reduces changes in the relative distribution of charged species of the antibody when subjected to thermal, agitation, and / or light stresses relative to a control composition comprising the antibody.

44. The composition of any one of claims 1-43, wherein the composition reduces and / or prevents changes to the appearance of the composition when subjected to thermal, agitation, and / or light stresses relative to a control composition comprising the antibody.

45. The composition of any one of claims 1-44, wherein the antibody comprises methionine or tryptophan in a complementarity determining region (CDR).

46. The composition of any one of claims 1-45, wherein the antibody is an anti- TMPRSS6 antibody.

47. The composition of any one of claims 1-46, wherein the antibody comprises at least one amino acid residue capable of undergoing a post-translational modification (PTM).

48. The composition of claim 47, wherein the PTM is pyro-glutamic acid, oxidation, isomerization, glycation, deamidation, or succinimide formation.

49. The composition of claim 48, wherein the oxidation is methionine oxidation and / or tryptophan oxidation.

50. The composition of claim 48, wherein the oxidation is di-oxidation.119#14616800v251. The composition of claim 50, wherein the di-oxidation is methionine di-oxidation, tryptophan di-oxidation, and / or histidine di-oxidation.

52. The composition of claim 48, wherein the deamidation is asparagine deamidation.

53. The composition of claim 52, wherein the asparagine deamidation occurs on the 326N residue of a heavy chain of the antibody.

54. The composition of claim 48, wherein the glycation is lysine glycation.

55. The composition of any one of claims 47-54, wherein the composition reduces and / or prevents the PTM.

56. The composition of any one of claims 1-55, wherein the antibody comprises an HC CDR1 having the amino acid sequence of SEQ ID NO: 24, an HC CDR2 having the amino acid sequence of SEQ ID NO: 48, an HC CDR3 having the amino acid sequence of SEQ ID NO: 26, an LC CDR1 having the amino acid sequence of SEQ ID NO: 27, an LC CDR2 having the amino acid sequence of WAT, and an LC CDR3 having the amino acid sequence of SEQ ID NO: 29.

57. The composition of any one of claims 1-56, wherein the antibody comprises a heavy chain variable domain having the amino acid sequence of SEQ ID NO: 49, and a light chain variable domain having the amino acid sequence of SEQ ID NO: 50.

58. The composition of any one of claims 1-56, wherein the antibody comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 52, and a light chain comprising the amino acid sequence of SEQ ID NO: 53.

59. A composition comprising:(i) 100 mM L-histidine monohydrochloride;(ii) 20mg / mL sucrose;(iii) 100 mM L-arginine monohydrochloride;(iv) 0.2mg / mL polysorbate 80; and(v) 150-175 mg / mL anti-TMPRSS6 antibody,120#14616800v2wherein the anti-TMPRSS6 antibody comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 52, and a light chain comprising the amino acid sequence of SEQ ID NO: 53.

60. A composition comprising:(i) 50 mM L-histidine monohydrochloride;(ii) 20mg / mL sucrose;(iii) 100 mM L-arginine monohydrochloride;(iv) 10 mM L-methionine monohydrochloride;(v) 0.2mg / mL polysorbate 80; and(vi) 150-175 mg / mL anti-TMPRSS6 antibody, wherein the anti-TMPRSS6 antibody comprises a heavy chain comprising the amino acid sequence of SEQ ID NO: 52, and a light chain comprising the amino acid sequence of SEQ ID NO: 53.

61. A prefilled syringe comprising the composition of any one of claims 1-60.

62. The prefilled syringe of claim 61, wherein the prefilled syringe is a glass prefilled syringe.121#14616800v2

Images