AQUEOUS STABLE ANTIBODY FORMULATIONS

Abstract

The present invention relates to a stable aqueous antibody formulation, characterized in that it comprises: a. 20 to 100 mg / mL of an antibody, wherein the antibody comprises a heavy chain comprising SEQ ID NO: 4 and a light chain comprising SEQ ID NO: 2; and b. approximately 0.003-0.3% of polysorbate-20 (ps-20); and c. a buffer; and d. 50 to 800 mM of trehalose, wherein the formulation has a pH of 5.0 to 7.5.

Description

The present invention relates to stable, aqueous antibody formulations. In some embodiments, the stable, aqueous formulations comprise from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and from approximately 0.002% to approximately 0.01% polysorbate-20. Methods for preparing and using such antibody formulations are also provided. Background of the Invention Antibodies have been used in the treatment of various diseases and conditions due to their specificity in recognizing their target, thus generating highly selective results after systemic administration. In order for antibodies to remain effective, they must maintain their biological activity during their production. C7QC Ln / Lznz / E / YILI purification, transport, and storage. New production and purification techniques have been developed to enable the production of large quantities of highly purified monoclonal antibodies. However, difficulties remain in stabilizing these antibodies for transport and storage, and even more so in providing the antibodies in a pharmaceutical form suitable for administration. Denaturation, aggregation, contamination, and particle formation can be significant obstacles in antibody formulation and storage. Due to the wide variety of antibodies, there are no universal conditions or formulations suitable for storing all antibodies. The optimal conditions and formulations for storing an antibody are often specific to that antibody. Therefore, antibody formulations and storage methods are often a significant part of the research and development process for a commercial antibody. Several methods have been proposed to address the difficulties associated with antibody stability. For example, in some cases, the antibody is often lyophilized and then reconstituted shortly before administration. However, reconstitution is not ideal. C7QC Lh / Lznz / E / YILI, as it adds an extra step to the administration process and could introduce contaminants into the formulation. Furthermore, even reconstituted antibodies can exhibit aggregation and particle formation problems. Therefore, there is a need to provide stable, aqueous antibody formulations that can overcome the challenges associated with transport and storage. Brief Description of the Invention The present invention relates to a stable, aqueous antibody formulation comprising: (A) from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and (B) from approximately 0.002% to approximately 0.01% of polysorbate-20. In some embodiments, the antibody formulation also includes an uncharged excipient. In some embodiments, the uncharged excipient is trehalose. In some embodiments, the concentration of uncharged excipient The loaded C7QC Ln / Lznz / E / YILI concentration is approximately 20 mM to approximately 80 mM. In some formulations, the unloaded excipient concentration is approximately 200 mM to approximately 400 mM. The antibody may be present in various concentrations. In some formulations, the concentration ranges from approximately 2 to approximately 20 mg / mL of the antibody. In some formulations, the concentration ranges from approximately 20 to approximately 100 mg / mL of the antibody. In one formulation, the concentration is 30 mg / mL of the antibody. The formulation may also include arginine. In some embodiments, the arginine is L-arginine. In some embodiments, the formulation comprises approximately 100 mM to approximately 200 mM of L-arginine. In some embodiments, the formulation comprises approximately 120 mM to approximately 140 mM of L-arginine, and approximately 40 mM to approximately 60 mM of uncharged excipient. In one embodiment, the formulation comprises approximately 125 mM L-arginine. In one embodiment, the formulation comprises approximately 130 mM L-arginine. In some formulations, the formulation also includes histidine. In some formulations, the histidine concentration is approximately 15 mM to approximately 30 mM. In one formulation, the histidine concentration is C7QC Ln / Lznz / Ε / ΥΙΛΙ approximately 20 mM. In some forms, the antibody was not subjected to lyophilization. In some embodiments, the invention relates to a stable, aqueous antibody formulation comprising from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, where the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and where the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the formulation is stable after storage at approximately 40°C for at least 1 month. In some embodiments, the formulation is stable after storage at approximately 25°C for at least 3 months. In some embodiments, the formulation is stable after storage at approximately 5°C for at least 18 months.In some formulations, the antibody stored at approximately 40°C for at least 1 month retains at least 80% of its IL-5R polypeptide binding capacity compared to an unstored reference antibody. In some formulations, the antibody stored at approximately 5°C for at least 6 months retains at least 80% of its IL-5R polypeptide binding capacity compared to an unstored reference antibody. In some formulations, the antibody stored at approximately 40°C for at least 1 month retains at least 95% of its IL-5R polypeptide binding capacity compared to an unstored reference antibody. In some formulations, the antibody stored at approximately 5°C for at least 6 months retains at least 95% of its IL-5R polypeptide binding capacity compared to an unstored reference antibody.In some formulations, less than 2% of the antibody forms an aggregate after storage at approximately 40°C for at least 1 month, as determined by HPSEC. In some formulations, less than 2% of the antibody forms an aggregate after storage at approximately 5°C for at least 12 months, as determined by HPSEC. In some embodiments, the formulation is substantially free of particles after storage at approximately 40°C for at least 1 month, as determined by visual inspection. In some embodiments, the formulation is substantially free of particles after storage at approximately 5°C for at least 12 months, as determined by visual inspection. In some modalities, the formulation is a C7QC Ln / Lznz / E / YILI injectable formulation. In some forms, the formulation is suitable for intravenous, subcutaneous, or intramuscular administration. In some embodiments, the invention relates to a sealed container holding an antibody formulation as described herein. In some embodiments, the invention relates to a pharmaceutical unit dosage form suitable for parenteral administration to a human, comprising an antibody formulation as described herein in a suitable container. In some embodiments, the antibody formulation is administered intravenously, subcutaneously, or intramuscularly. In some embodiments, the suitable container is a pre-filled syringe. In some embodiments, the pre-filled syringe comprises a needle. In some embodiments, the needle is a 29G thin-walled needle. In some embodiments, the pre-filled syringe is a plastic syringe or a glass syringe. In some embodiments, the pre-filled syringe is made of materials that are substantially tungsten-free. In some embodiments, the pre-filled syringe is coated with silicone. In some embodiments, the pre-filled syringe comprises a plunger having a fluoropolymer resin disc. In some embodiments, the pre-filled syringe comprises (a) approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, where the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and where the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and (b) approximately 0.002% to approximately 0.01% of polysorbate-20.In some embodiments, the pre-filled syringe further comprises: (c) approximately 40 mM to approximately 60 mM of trehalose, and (d) approximately 110 mM to approximately 150 mM of L-arginine. In some embodiments, the invention relates to a pre-filled syringe comprising: (a) approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 8-10, and (b) approximately 0.002% to approximately 1. 0.01% polysorbate-20. In some embodiments, the formulation further comprises: (c) approximately 200 mM to approximately 300 mM of trehalose. In some embodiments, the invention relates to a kit comprising the formulation described herein, the container described herein, the unit dosage forms described herein, or the pre-filled syringes described herein. In some embodiments, the invention relates to a stable, aqueous antibody formulation comprising: (a) approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, where the heavy-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 5-7, and where the light-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.002% to approximately 0.01% of polysorbate-20, (c) approximately 40 mM to approximately 60 mM of trehalose, (d) approximately 110 mM to approximately 150 mM of L-arginine, and (e) approximately 15 to approximately 30 mM of histidine.In one embodiment, the invention relates to a stable, aqueous antibody formulation comprising: (A). C7QC Ln / Lznz / E / YILI from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.006% of polysorbate-20, (c) approximately 50 mM of trehalose, (d) approximately 130 mM L-arginine and (e) approximately 20 mM of histidine. In some embodiments, the invention relates to a stable, aqueous antibody formulation comprising: (a) from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) from approximately 0.002% to approximately 0.01% of polysorbate-20, (c) from approximately 200 mM to approximately 300 mM of trehalose, and (d) from approximately 15 to approximately 30 mM of histidine.In one embodiment, the invention relates to a stable, aqueous antibody formulation comprising: (A) from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.006% polysorbate-20, (c) approximately 250 mM trehalose, and (d) approximately 20 mM histidine.In another embodiment, the invention relates to a stable, aqueous antibody formulation comprising: (a) approximately 30 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, where the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and where the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.006% polysorbate-20, (c) approximately 250 mM trehalose, and (d) approximately 20 mM histidine. In some embodiments, the invention relates to a method of producing a stable, aqueous antibody formulation, the method comprising: (a) purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; (b) placing the isolated antibody into a stabilizing formulation to form a stable, aqueous antibody formulation, wherein the resulting stable, aqueous antibody formulation comprises: (i) from approximately 2 mg / ml to approximately 100 mg / ml of the antibody, and (ii) approximately 0.002% to approximately 0.01% polysorbate-20. In some embodiments, the invention relates to a method of preparing a stable, aqueous antibody formulation, the method comprising: (A) purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy chain variable region and a chain variable region C7QC Ln / Lznz / E / YILI light, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the region C7QC Ln / Lznz / E / YILI light chain variable comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; (b) diluting the antibody from approximately 2 mg / ml to approximately 20 mg / ml of the antibody in a solution comprising: (i) approximately 0.002% to approximately 0.01% of polysorbate-20, (ii) approximately 40 mM to approximately 60 mM of trehalose, and (iii) approximately 110 mM to approximately 150 mM of L-arginine. In some embodiments, the invention relates to a method of preparing a stable, aqueous antibody formulation, the method comprising: (a) purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; (b) diluting the antibody from approximately 20 mg / ml to approximately 100 mg / ml of the antibody in a solution comprising: (i) approximately 0.002% to approximately 0.01% of polysorbate-20, and (ii) approximately 200 mM to approximately 300 mM of trehalose. In some embodiments, the invention relates to a method of producing a reconstituted antibody formulation comprising an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, the method comprising: (a) purifying the antibody from a cell culture; (b) lyophilizing the isolated antibody; (c) adding the lyophilized antibody to an aqueous solution to form a reconstituted antibody formulation, wherein the reconstituted antibody formulation comprises: (i) from approximately 2 mg / ml to approximately 100 mg / ml of the antibody, and (ii) approximately 0.002% to approximately 0.01% polysorbate-20. In some embodiments, the invention relates to an antibody formulation comprising an antibody, in the C7QC Ln / Lznz / E / YILI wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially particle-free.In some embodiments, the antibody formulation comprises an antibody comprising a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially free of active glutathione S-transferase (GST). In some embodiments, the antibody formulation is essentially free of GST. In some embodiments, the antibody formulation is essentially free of particles for at least 1 month when stored at 38-42°C. In some embodiments, the antibody formulation is essentially free of particles for at least 6 months when stored at 2-6°C.In some modalities, the antibody formulation is essentially particle-free for at least 18 months when stored at 26°C. In some embodiments, the invention relates to a method for purifying an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, the method comprising: (a) obtaining a cell culture comprising the antibody, (b) performing affinity chromatography on the antibody, (c) performing cation exchange on the antibody, and (d) performing mixed-mode chromatography on the antibody. In some embodiments, the method further comprises a virus deactivation process and / or a diafiltration process. In some embodiments, the invention relates to a method of treating a pulmonary disease or disorder in a subject, the method comprising administering a therapeutically effective quantity of the antibody formulations described herein, the containers C7QC Ln / įZРZ / B / YILI described herein, the unit dosage forms described herein, or the pre-filled syringes described herein. In some modalities, the pulmonary disease or disorder is an eosinophilic disease or disorder. In some cases, the pulmonary disease or disorder is asthma, COPD, eosinophilic asthma, combined eosinophilic and neutrophilic asthma, aspirin-responsive asthma, allergic bronchopulmonary aspergillosis, acute and chronic eosinophilic bronchitis, acute and chronic eosinophilic pneumonia, Churg-Strauss syndrome, hypereosinophilic syndrome, pulmonary eosinophilia induced by drugs, irritants, and radiation, pulmonary eosinophilia induced by infection (fungi, tuberculosis, parasites), autoimmune-related pulmonary eosinophilia, eosinophilic esophagitis, Crohn's disease, or a combination thereof. In some cases, the pulmonary disease or disorder is asthma.In some forms, the lung disease or disorder is chronic obstructive pulmonary disease (COPD). Brief Description of the Figures Figure 1. Amino acid sequences of anti-IL5R antibody. Figure 2 shows the effect of polysorbate-20 on the monomer fraction in solution. A polysorbate concentration above 0.005% is required for C7QC Ln / Lznz / E / YILI fully maintain the monomer level. Figure 3 shows the effect of polysorbate-20 on subvisible particle counts in 2 g / L solutions. Data for particles > 2 pm are not shown, but they exhibit a similar pattern to the larger particles. The data indicate that subvisible particle levels in 2 g / L solutions are not controlled by any level of polysorbate. Figure 4 shows the effect of polysorbate-20 on subvisible particle counts in 100 g / L solutions. Data for particles > 2 pm are not shown, but they exhibit a similar pattern to the larger particles. The data indicate that polysorbate levels above 0.003% control subvisible particle levels in 100 g / L solutions. Figure 5. HPLC monomer (%) and other results (%) as a function of solution pH and protein concentration. Monomer loss is minimized in the pH range of 5.5–6.5. Figure 6. Particle formation, including subvisible particles > 10 pm measured by MFI and visible particles assessed by comparison with standards, as a function of solution pH and protein concentration. Subvisible particle counts depend on protein concentration but do not show a trend. C7QC Ln / Lznz / E / YILI clear with pH. More visible particles are observed in solutions of lower protein concentration in the pH range of 5.5-6.5. Figure 7. Subvisible particle counts > 10 pm, filtered aspect ratio to remove silicone oil droplets. Data compare SVP counts immediately after shipment with those after 1 month of storage at 25°C. High counts are observed for low protein concentrations, independent of PS-20. Figure 8. Particle counts >10 pm by MFI after simulated transport for varying protein formulations and concentrations. Higher ionic strength formulations are more stable than trehalose formulations > 10 g / L. Figure 9. Particle counts >10 pm by MFI after simulated transport for variable and 2 g / 1 protein formulations. Arginine concentration must be > 50 mM and NaCl concentration must be > 75 mM. Figure 10. Particle counts >10 pm by MFI after simulated transport for variable and 2 g / 1 protein formulations. Any excipient concentration in this range is acceptable. Figure 11. Particle counts >10 pm by MFI after simulated transport for variable and 2 g / 1 protein formulations. Figures 12A-12C show the monomer loss for the 2 mg / ml, 20 mg / ml, and 100 mg / ml formulations in vials and pre-filled syringes. All pre-filled syringes show similar loss with respect to the vials and to each other. Figure 13 shows the graphical representation of the pooling strategy. Blue indicates formulations containing arginine or NaCl. Green indicates the trehalose formulation. Data points represent prepared samples, and lines indicate the available pooled options for achieving intermediate doses. Figure 14. The test plan for Stability Study No. 2. All marked tests will be performed on the antibody formulation. Yellow shading indicates that the test will be performed on the placebo. The ABC notation indicates submission to the following tests: potency (BIOASSAY), RP-HPLC, cIEF, non-reduced bioanalyzer, and reduced bioanalyzer. Figure 15 is a graph showing samples prepared to define the design space as a function of protein and polysorbate-20 (PS-20) concentrations for formulation groupings. Figure 16 is a graph of subvisible particles using MFI at time 0, after shipment. The results show that particles form if PS-20 is not present, but 0.002% PS-20 is sufficient to inhibit the C7QC Ln / ίZΖΠΖ / E / YΙΛΙ particle formation after shipment. Figures 17A-17D. Observations of visible particles are scored against appearance patterns and are shown here at the 9-month time point. Observations were made very close to the light source. The samples shown include pre-filled syringes (PFS) containing the trehalose formulation (Figure 17A), vials containing the trehalose formulation (Figure 17B), PFS containing the arginine formulation (Figure 17C), and vials containing the arginine formulation (Figure 17D). The data support a target of 0.006% PS-20 and an acceptable range of 0.002–0.01% PS-20 in PFS. The vials are shown as a worst-case comparison. Figure 18 compares various SVP methods for capturing an increase with sampling time, which correlates with visible particles. Flow cytometry and small particle counts (>1 and >2 pm) by MFI can capture the trend well. Figures 19A and 19B compare appearance pattern scores and MFI results (particles > Ipm) for trehalose formulations in PFS (Figure 19A) and vials (Figure 19B). Good agreement is observed between the two methods, both indicating that the acceptable PS-20 range is 0.002–0.01%. Figure 20 represents such a clustering design C7QC Ln / ίZРZ / Β / YΙΛΙ as briefly explained in Example 3 and the leading batch stability study conducted at ABC. The orange shaded area indicates the arginine formulation and the blue shaded area indicates the trehalose formulation, both with 0.006% PS-20. Figure 21 represents a schematic example of an antibody purification process. Figure 22 represents the two-dimensional gel analysis of the unretained fraction of a protein-A column used in the purification of anti-IL5R antibody. Detailed Description of the Invention It should be noted that the specific implementations shown and described herein are examples and are not intended to limit the scope of the application in any way. It should also be noted that each of the embodiments and features of the invention described herein may be combined in any and all ways. The published patents, patent applications, websites, company names, and scientific bibliography mentioned herein are incorporated herein by reference in their entirety, in the same manner as if each were specifically and individually indicated as being incorporated by reference. Any conflict between any references cited herein and the C7QC Ln / Lznz / E / YILI specific content of this descriptive memorandum shall be resolved in favor of the latter. Likewise, any conflict between a definition of a term or expression as interpreted in the art and a definition of the term or expression as specifically stated in this descriptive memorandum shall be resolved in favor of the latter. The singular forms un, uno / ay el / la, as used in this descriptive record, also specifically encompass the plural forms of the terms they refer to, unless the content clearly indicates otherwise. Throughout this document, all expressions of percentage, ratio, and the like are by weight, unless otherwise stated. The expression by weight, as used herein, is synonymous with the expression by mass and indicates that a ratio or percentage defined herein is obtained according to weight rather than volume, thickness, or any other measure. The term "approximately" is used herein to refer to roughly, in the region of, more or less, or around. When the term "approximately" is used in conjunction with a numerical interval, it modifies the interval by extending its limits above and below the stated numerical values. In general, the term "approximately" is used herein to modify a numerical value above and below the stated value with a variance of 10%. The technical and scientific terms used herein have the meanings customarily assigned to a person skilled in the art to which this application pertains, unless otherwise defined. Reference is made herein to various methodologies and materials known to those skilled in the art. Standard reference works that set forth the general principles of recombinant DNA technology include Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd ed., Coid Spring Harbor Laboratory Press, New York (1989); Kaufman et al., eds., Handbook of Molecular and Cellular Methods in Biology and Medicine, CRC Press, Boca Raton (1995); and McPherson, ed., Directed Mutagenesis: A Practical Approach, IRL Press, Oxford (1991), descriptions of each of which are incorporated herein by reference in their entirety. The present invention relates to stable, aqueous antibody formulations. The term "antibody formulation," as described herein, refers to a composition comprising one or more antibody molecules. The term "antibody" is not particularly limited in the present invention. For clarity, "antibody" is considered in its broadest sense and includes any immunoglobulin (Ig), active variants, or The term antibody can also refer to dimers or multimers. Antibodies can be polyclonal or monoclonal and can be of natural origin or recombinantly produced. Thus, the term antibody encompasses all human, non-human, humanized, and chimeric antibodies. Typically, an antibody is a monoclonal antibody of one of the following classes: IgG, IgE, IgM, IgD, or IgA; and most commonly, it is IgG or IgA. An antibody of the invention may be of any animal origin, including mammals and birds. In some embodiments, the antibody of the methods of the invention is human, murine (e.g., mouse and rat), donkey, sheep, rabbit, goat, guinea pig, camel, horse, or chicken. Human antibodies, as used herein, include antibodies containing the amino acid sequence of a human immunoglobulin and include antibodies isolated from human immunoglobulin collections or from animals transgenic for one or more human immunoglobulins and that do not express endogenous immunoglobulins. See, e.g., U.S. Patent No. 5,939,598 to Kucherlapati et al. An antibody of the invention may include, e.g. e.g., native antibodies, intact monoclonal antibodies, polyclonal antibodies, multispecific antibodies (e.g., bispecific antibodies) formed from at least two intact antibodies, antibody fragments (e.g., antibody fragments that recognize and / or bind to one or more antigens), humanized antibodies, human antibodies (Jakobovits et al., Proc. Nati. Acad. Sci. USA 90:2551 (1993); Jakobovits et al., Nature 362:255-258 (1993); Bruggermann et al., Year in Immunol. 7:33 (1993); U.S. Patents Nos. 5,591,669 and 5,545,807), antibodies and antibody fragments isolated from antibody foci collections (McCafferty et al., Nature 348:552-554) (1990); Clackson et al., Nature 352:624-628 (1991); Marks et al., J. Mol. Biol. 222:581-597 (1991); Marks et al., Bio / Technology 10:779-783 (1992); Waterhouse et al., Nucí. Acids Res. 21:2265-2266 (1993)).An antibody purified by the method of the invention can be recombinantly fused to a heterologous polypeptide at the N or C terminus or can be chemically conjugated (including covalent and non-covalent conjugations) to polypeptides or other compositions. For example, an antibody purified by the method of the present invention can be recombinantly fused or conjugated to molecules useful as markers in screening assays and effector molecules such as heterologous polypeptides, drugs, or toxins. Refer, e.g., to PCT publications WO 92 / 08495, WO 91 / 14438, WO 89 / 12624; U.S. Patent No. 5,314,995; and EP 396,387. In some embodiments, the antibody formulation of the present invention comprises an anti-IL5 receptor antibody (anti-IL5R). The antibodies of the present invention bind specifically to an antigen of interest or a fragment thereof, and do not bind specifically to other antigens or fragments thereof. For example, an anti-IL5R antibody will bind immunospecifically to an interleukin-5 receptor-like polypeptide and will not bind specifically to other polypeptides. Preferably, the antibodies or antibody fragments that bind immunospecifically to an IL-5 receptor have a higher affinity for an IL-5 receptor or an IL-5 receptor-like polypeptide fragment compared to their affinity for other polypeptides or fragments of other polypeptides.The affinity of an antibody is a measure of its binding to a specific antigen at a single antigen-antibody site and is essentially the sum of all the attractive and repulsive forces present in the interaction between the antigen-binding site of an antibody and a particular epitope. The affinity of an antibody for a particular antigen (e.g., an IL-5-like polypeptide or a fragment of an IL-5-like polypeptide) can be expressed by the equilibrium constant K, defined by the equation K = [Ag Ac] / [Ag] [Ac], which corresponds to the affinity of the antibody's binding site, where [Ag] is the concentration of free antigen, [Ac] is the concentration of free antibody, and [Ag Ac] is the concentration of the antigen-antibody complex. When the antigen and antibody react intensely with each other, there will be very little free antigen or free antibody, and therefore the equilibrium constant or antibody affinity will be high.High-affinity antibodies are found in which there is a good fit between the antigen and the antibody (for a discussion regarding antibody affinity, see Sigal and Ron ed., 1994, Immunology and Inflammation: Basic Mechanisms and Clinical Consequences, McGraw-Hill, Inc., New York, pp. 56–57; and Seymour et al., 1995, Immunology: An Introduction for the Health Sciences, McGraw-Hill Book Company, Australia, pp. 31–32). Preferably, antibodies or antibody fragments that bind immunospecifically to an IL-5-like polypeptide or a fragment thereof do not cross-react with other antigens. That is, antibodies or antibody fragments that bind immunospecifically to an IL-5-type polypeptide or a fragment thereof with higher energy than to other polypeptides or fragments of other polypeptides (refer, e.g., to Paul ed., 1989, Fundamental Immunology, 2nd ed., Raven Press, New York). (See pages 332-336 for a discussion of antibody specificity). Antibodies or antibody fragments that bind immunospecifically to an IL-5-like polypeptide can be identified, for example, by immunoassays such as radioimmunoassays (RIA), enzyme-linked immunosorbent assays (ELISA), and BIAcore assays, or other techniques known to those skilled in the art (refer, e.g., to Seymour et al., 1995, Immunology - An Introduction for the Health Sciences, McGraw-Hill Book Company, Australia, pages 33-41 for a discussion of various assays for determining antibody-antigen interactions in vivo). Antibodies or antibody fragments that bind immunospecifically to an IL-5-like polypeptide or a fragment thereof only antagonize an IL-5-like polypeptide and do not significantly antagonize other activities. In one embodiment, an IL-5R-like polypeptide is human IL-5R, an analogue, derivative, or fragment thereof. The nucleotide sequence of human IL-5R can be found in the GenBank database (see, for example, Registry No. M96652.1). The amino acid sequence of human IL-5R can be found in the GenBank database (see, for example, Registry No. Q01344). Each of these registry numbers is expressly incorporated herein by reference. C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ In some embodiments, the antibody formulation comprises an anti-IL5R antibody, for example, a human anti-IL5R antibody. In some embodiments, the anti-IL5R antibody comprises a light chain comprising SEQ ID NO: 2 and a heavy chain comprising SEQ ID NO: 4. In some further embodiments, the anti-IL5R antibody comprises a light chain variable region comprising SEQ ID NO: 1 and a heavy chain variable region comprising SEQ ID NO: 3. In one further embodiment, the anti-IL5R antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 8-10.Those knowledgeable in the technique could easily identify the CDRs according to the Chothia, Abm or other numbering systems. In one embodiment, the anti-IL5R antibody is benralizumab. Information regarding benralizumab (or fragments thereof) for use in the methods provided herein can be found in the publication of United States Patent Application No. US 2010 / 0291073 A1, the description of which is incorporated herein in full by reference. The term "analogue" or "analogue of an antibody," as used herein in the context of an antibody, refers to a second antibody, i.e., an antibody analogue, which has similar or identical functions to the antibody, but does not necessarily comprise a sequence of amino acids similar or identical to that of the antibody, nor does it have a structure similar or identical to that of the antibody. An antibody having a similar amino acid sequence refers to an antibody analogue that satisfies at least one of the following criteria: (a) an antibody analogue having an amino acid sequence with an identity of 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 at least 99% with respect to the amino acid sequence of the antibody;(b) an analogue of the antibody encoded by a nucleotide sequence that hybridizes under rigorous conditions with a nucleotide sequence encoding the antibody of at least 5 contiguous amino acid residues, at least 10 contiguous amino acid residues, at least 15 contiguous amino acid residues, at least 20 contiguous amino acid residues, at least 25 contiguous amino acid residues, at least 40 contiguous amino acid residues, at least 50 contiguous amino acid residues, at least 60 contiguous amino acid residues, at least 70 contiguous amino acid residues, at least 80 contiguous amino acid residues, at least 90 contiguous amino acid residues, at least 100 contiguous amino acid residues, at least 125 contiguous amino acid residues, or at least 150 amino acid residues contiguous; and (c) an antibody analogue encoded by a nucleotide sequence having at least 30%, at least 35%, or at least one identity; 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 at least 99% of the nucleotide sequence encoding the antibody. An antibody analog with a structure similar to that of the antibody refers to a proteinaceous agent that has a secondary, tertiary, or quaternary structure similar to that of the antibody. The structure of an antibody or an antibody analog can be determined using methods known to those skilled in the art, including, but not limited to, peptide sequencing, X-ray crystallography, nuclear magnetic resonance, circular dichroism, and crystallographic electron microscopy. To determine the percentage of identity between two amino acid or nucleic acid sequences, the sequences are aligned for optimal comparison (e.g., gaps can be introduced into the sequence of a first amino acid or nucleic acid sequence for optimal alignment with a second amino acid or nucleic acid sequence). The amino acid residues or nucleotides at corresponding amino acid or nucleotide positions are then compared. When a position in the first sequence is occupied by the same amino acid residue or nucleotide as the corresponding position in the second sequence, then the molecules are identical at that position.The percentage of identity between the two sequences is a function of the number of identical positions shared by the sequences (i.e., % identity = number of identical overlapping positions / total number of positions x 100%). In one modality, the two sequences have the same length. Determining the percentage of identity between two sequences can also be done using a mathematical algorithm. A non-limiting example of a mathematical algorithm used for comparing two sequences is the algorithm of Karlin and Altschul, 1990, Proc. Nati. Acad. Sci. USA 87:2264-2268, modified as in Karlin and Altschul, 1993, Proc. Nati. Acad. Sci. USA Science 90:5873-5877. A C7QC Ln / I 7P7 / B / YILI algorithm of this type is incorporated in the NBLAST and XBLAST programs of Altschul et al., 1990, J. Mol. Biol. 215:403. Nucleotide searches can be performed in BLAST with the parameters of the NBLAST nucleotide program set, e.g., for a score = 100 and a word length = 12, in order to obtain nucleotide sequences homologous to a nucleic acid molecule of the present invention. Protein searches can be performed in BLAST with the parameters of the XBLAST program set, e.g., for a score = 50 and a word length = 3, in order to obtain amino acid sequences homologous to a protein molecule of the present invention. In order to obtain gap alignments for comparative purposes, Gapped BLAST can be used as described in Altschul et al., (1997) Nucleic Acids Res. Science 25:33893402.Alternatively, PSI-BLAST can be used to perform an iterated search that detects distant correlations between molecules (Id). When using the BLAST, Gapped BLAST, and PSI-BLAST programs, the default parameters of the respective programs (e.g., XBLAST and NBLAST) can be used (refer, e.g., to the NCBI website). Another preferred, non-limiting example of a mathematical algorithm used for sequence comparison is the algorithm of Myers and Miller, 1988, CABIOS 4:11-17. Such an algorithm is incorporated into the ALIGN program (version 2.0). C7QC Ln / Lznz / E / YILI is part of the GCG sequence alignment software package. When using the ALIGN program to compare amino acid sequences, a PAM120 weight residue table, a gap length penalty of 12, and a gap penalty of 4 can be used. In some embodiments, the antibody in the antibody formulation is purified before being added to the antibody formulation. The terms isolate and purify refer to separating the antibody from an impurity or other contaminants in the composition in which the antibody resides, e.g., a composition comprising host cell proteins. In some embodiments, at least 50%, 70%, 80%, 90%, 95%, 98%, 99%, 99.5%, or 99.9% (w / w) of an impurity is purified from the antibody. For example, in some embodiments, the purification of the antibody, e.g., an anti-IL5R antibody, would comprise separating the antibody from 99% (w / w) of the host cell proteins originally present in the composition. In some modalities, the terms isolate and purify refer to separating an antibody, e.g., an anti-IL5R antibody, from an impurity or other contaminants in the composition to a degree that conforms to the guidelines of a governmental organization, e.g., the World Health Organization or the Food and Drug Administration. C7QC Lh / ίZΖΠΖ / Β / YΙΛΙ Foods from the United States. Those skilled in the technique will be familiar with antibody purification methods. Suitable purification techniques include various types of chromatography, such as affinity chromatography, hydrophobic interaction, ion exchange (such as cation exchange chromatography or mixed-mode chromatography), and filtration. Affinity chromatography refers to a separation method in which an antibody, by virtue of its specific binding properties, binds to a ligand with affinity for the antibody. The functional affinity ligand can be immobilized on a solid or semisolid support, such that when a composition comprising the antibody is passed through the ligand and the solid support, the antibody, having a specific binding affinity for the ligand, adsorbs to the ligand, and one or more different impurities do not adsorb (or bind with lower affinity) and are separated from the antibody. Examples of impurities that do not normally bind (or do not bind well) include process-related impurities (e.g., host cell proteins, DNA, medium components) and some product-related impurities (e.g., antibody fragments).In some embodiments, the solid support comprising the ligand is washed one or more times with a buffer to remove additional impurities before the adsorbed antibody is released from the ligand and support. After one or more impurities have been removed, the adsorbed antibody can be released (eluted) from the ligand and support, resulting in the isolation of the antibody from the original composition. The methods for releasing the antibody from the ligand and support depend on the ligand and are known to those skilled in the art and may include, for example, changes in the environment, such as pH, the addition of chaotropic or denaturing agents, or the addition of elution lamps that can be purchased from commercial suppliers. In some embodiments, more than one purification process may be employed on an antibody composition.Various affinity ligands are known in the technique, including protein A and protein G (and combinations thereof). Immobilized ligands are commercially available. For example, protein A affinity systems include MabSelect, MabSelect SuRe, MabSelect Xtra, MabSelect SuRe LX, Sepaharose CL-4B, ProSep vA, ProSep vA Ultra, and Ceramic HyperD. Ion-exchange chromatography includes cation-exchange chromatography and mixed chromatography. Cation-exchange chromatography refers to any method by which an antibody and some C7QC Ln / įZРZ / B / YILI Impurity or impurities can be separated based on charge differences using a cation exchange matrix. A cation exchange matrix generally comprises covalently bonded, negatively charged groups. Strong or weak cation exchange resins can be employed. Typically, strong cation exchange resins comprise supported organic groups consisting of sulfonate or sulfonic acid groups, depending on the pH. Weak cation exchange resins typically comprise supported organic groups consisting of carboxylate or carboxylic acid groups, depending on the pH. In certain embodiments, multimodal cation exchange resins can be used, which incorporate additional bonding mechanisms as well as additional ionic interactions, for example, one or more hydrogen bonding and hydrophobic interactions.Examples of suitable cation-exchange resins are well-known in the art and may include, but are not limited to, a Fractogel matrix, carboxymethyl (CM), sulfoethyl (SE), sulfopropyl (SP), phosphate (P), and sulfonate (S), PROPAC WCX-10™ (Dionex), Capto S, S-Sepharose FF, Fractogel EMD SO3M, Toyopearl Megacap II SP 550C, Poros 50 HS, and SP-Sepharose. In some formulations, more than one cation-exchange chromatography process may be employed in the composition. Mixed-mode chromatography refers to a method that C7QC Ln / I 7P7 / B / YILI uses more than one form of interaction between the stationary phase and the analytes in order to achieve their separation from impurities (e.g., process-related impurities such as host cell proteins, DNA, and / or endogenous or adventitious viruses). Examples of suitable anion-exchange matrices are known in the technique and may include, but are not limited to, Capto Adhere, Sartobind Q, Natrix Q, Chromasorb Q, and Mustang Q. In some modalities, additional filtration stages can be used to remove impurities. For example, nanofiltration or ultrafiltration is used in some modalities. Nanofiltration involves passing the composition through a matrix with a pore size of, for example, less than 75 nm, less than 50 nm, or even less than 15 nm, to separate impurities, such as viruses, from the antibody. Commercial nanofilters and ultrafilters that can be used are produced by various suppliers, such as Millipore Corporation (Billerica, Mass., for example, Viresolve Pro and Viresolve Pro+), Pall Corporation (East Hills, NY), GE Healthcare Sciences (Piscataway, NJ), and Sartorius Corporation (Göttingen, Germany). In some embodiments, the antibody of the present invention, for example, an anti-IL5R antibody comprising a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, is available in concentrations of 1 mg / ml to 200 mg / ml, 2 mg / ml to 100 mg / ml, 2 mg / ml to 30 mg / ml, 2 mg / ml to 2.5 mg / ml, 2 mg / ml to 2.0 mg / ml, 3 mg / ml, 4 mg / ml, 5 mg / ml, 6 mg / ml, 7 mg / ml, 8 mg / ml, 9 mg / ml, 10 mg / ml, 11 mg / ml, 12 mg / ml, 13 mg / ml, 14 mg / ml, 15 mg / ml, 16 mg / ml, 17 mg / ml, 18 mg / ml, 19 mg / ml or 20 mg / ml.In some embodiments, the antibody of the present invention, for example, antiIL5R, has a concentration of approximately 20 mg / ml, 25 mg / ml, 30 mg / ml, 40 mg / ml, 45 mg / ml, 50 mg / ml, 55 mg / ml, 60 mg / ml, 65 mg / ml, 70 mg / ml, 75 mg / ml, 80 mg / ml, 85 mg / ml, 90 mg / ml, 95 mg / ml or 100 mg / ml. The antibody formulation of the present invention may comprise an uncharged excipient. The term excipient refers to a pharmacologically inactive substance formulated with the antibody as described herein. In some embodiments, the excipient may aid in preventing denaturation or otherwise assist in stabilizing the antibody. Suitable excipients for use in pharmaceutical compositions are known in the art. Examples may be taken from the manual: Gennaro, Alfonso R.: Remington's Pharmaceutical Sciences, Mack Publishing Company, Easton, PA, 1990. In some embodiments, the excipient is an uncharged excipient, i.e., the excipient does not carry a positive or negative charge. In some embodiments, the C7QC Ln / ίΖΠΖ / Β / ΥΙΛΙ excipient is selected from the group consisting of fructose, Glucose, maltose, sorbose, xylose, lactose, maltose, sucrose, dextran, pullulan, dextrin, cyclodextrins, soluble starch, trehalose, sorbitol, erythritol, isomalt, lactitol, xylitol, glycerol, lactitol, hydroxyethyl starch, water-soluble glucans. In some formulations, the uncharged excipient is approximately 1 mM to approximately 1 M, approximately 2 mM to approximately 500 mM, approximately 5 mM to approximately 400 mM, approximately 10 mM to approximately 300 mM, or approximately 20 mM to approximately 250 mM in the antibody formulation. In some embodiments, the unloaded excipient is at approximately 5 mM to approximately 150 mM, approximately 10 mM to approximately 100 mM, approximately 20 mM to approximately 80 mM, approximately 30 mM to approximately 40 mM, approximately 50 mM to approximately 60 mM, or approximately 70 mM in the antibody formulation, for example, an antibody formulation comprising 2 to 20 mg / ml antibody. In one embodiment, the unloaded excipient is at approximately 50 mM in the antibody formulation. In some embodiments, C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ The unloaded excipient is at approximately 50 mM to approximately 800 mM, approximately 100 mM to approximately 500 mM, approximately 150 mM to approximately 400 mM, approximately 200 mM to approximately 400 mM, approximately 200 mM to approximately 300 mM, or approximately 250 mM in the antibody formulation, for example, an antibody formulation comprising 20 to 100 mg / ml antibody. In one embodiment, the unloaded excipient is at approximately 250 mM in the antibody formulation. In some formulations, the uncharged excipient is trehalose, as represented by the formula: OH In some forms, trehalose is available from approximately 1 mM to approximately 1 M, from approximately 2 mM to approximately 500 mM, from approximately 5 mM to approximately 400 mM, from approximately 10 mM to approximately 300 mM or approximately 20 mM to approximately 250 mM in the antibody formulation. In some embodiments, trehalose is approximately 5 mM to approximately 150 mM, approximately 10 mM to approximately 100 mM, approximately 20 mM to approximately 80 mM, approximately 30 mM to approximately 40 mM, approximately 50 mM to approximately 60 mM, or approximately 70 mM in the antibody formulation, for example, an antibody formulation comprising antibody concentrations of 2 to 20 mg / ml. In one embodiment, trehalose is approximately 50 mM in the antibody formulation. In some embodiments, trehalose is approximately C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ about 50mM to about 800mM, about 100mM to about 500mM, about 150mM to about 400mM, about 200mM to about 400mM, about 200mM to about 300mM, or approximately 250 mM in the antibody formulation, for example, an antibody formulation comprising 20 to 100 mg / ml of antibody. In one embodiment, trehalose is at approximately 250 mM in the antibody formulation. The antibody formulation of the present invention comprises arginine. Arginine is a conditionally non-essential amino acid that can be represented by the formula: C7QC Ln / I 7Π7 / Β / YILI NH ( Arginine, as used herein, may include the free-base form of arginine, as well as any and all of its salts. In some embodiments, arginine includes a pharmaceutically acceptable salt thereof. For example, arginine would include arginine hydrochloride. Arginine, as used herein, also includes all of its enantiomers (e.g., L-arginine and S-arginine) and any combination of enantiomers (e.g., 50% L-arginine and 50% sarginine; 90%–100% L-arginine and 10%–0% sarginine, etc.). In some embodiments, the term arginine includes more than 99% L-arginine and less than 1% S-arginine. In some embodiments, the term arginine includes enantiomerically pure L-arginine. In some forms, the arginine is a pharmaceutical-grade arginine. There may be several concentrations of arginine present in the antibody formulation. In some formulations, the antibody formulation comprises more than 50 mM arginine, more than 75 mM arginine, more than 100 mM arginine, more than 125 mM arginine, more than 130 mM arginine, more than 150 mM arginine, more than 175 mM arginine, or more than 200 mM arginine. In some formulations, the antibody formulation comprises up to 800 mM arginine, up to 600 mM arginine, up to 400 mM arginine, up to 200 mM arginine, up to 150 mM arginine, up to 130 mM arginine, or up to 125 mM arginine. In some formulations, the antibody formulation comprises 50 mM to 300 mM, 75 mM to 250 mM, 100 mM to 200 mM, 110 mM to 160 mM, 120 mM to 150 mM, or approximately 125 mM arginine. In some formulations, the antibody formulation comprises 125 mM arginine. In some formulations, the antibody formulation comprises 130 mM arginine. In some formulations, arginine is added in sufficient quantity to maintain the osmolarity of the formulation. In some formulations, arginine is added in sufficient quantity to achieve a hypertonic solution.Applicants have found that, in some modalities, an increase in the ionic strength of antibody formulations provides increased stability and a reduction in particle formation. The antibody formulations described herein may exhibit various viscosities. Methods for measuring the viscosity of antibody formulations are known to those skilled in the art and may include, e.g. C7QC Ln / I 7P7 / B / YILI e.g., a rheometer (e.g., an Anton Paar MCR301 rheometer with a 50 mm, 40 mm, or 20 mm plate attachment). In some embodiments of the present invention, viscosities are recorded with a high shear limit of 1000 per second for the shear rate. In some embodiments, the antibody formulation exhibits a viscosity of less than 20 centipoise (cP), less than 18 cP, less than 15 cP, less than 13 cP, or less than 11 cP. In some embodiments, the antibody formulation exhibits a viscosity of less than 13 cP. A person skilled in the art will appreciate that viscosity depends on temperature; therefore, unless otherwise specified, the viscosities provided herein are measured at 25°C. The term injection force refers to the amount of pressure (in Newtons) required to force the antibody formulation through a needle. Injection force correlates with the amount of resistance the antibody formulation provides when administered to a subject. Injection force depends on the gauge of the needle used for administration, as well as the temperature. In some modalities, the antibody formulation exhibits an injection force of less than 15 N, 12 N, 10 N, or 8 N when passed through a needle. C7QC Lh / įZРZ� / B / YILI of 27 Ga thin-walled PFS. In some modalities, the antibody formulation exhibits an injection force of less than 15 N, 12 N, 10 N or 8 N when passed through a 29 Ga thin-walled PFS needle. Antibody formulations can have different osmolarity concentrations. Methods for measuring the osmolarity of antibody formulations are known to those skilled in the art and may include, for example, an osmometer (e.g., an Advanced Instrument Inc. 2020 freezing point depression osmometer). In some formulations, the osmolarity ranges from 200 to 600 mOsm / kg, from 260 to 500 mOsm / kg, or from 300 to 450 mOsm / kg. The antibody formulation of the present invention may have different pH levels. In some embodiments, the pH of the antibody formulation is between 4 and 7, between 4.5 and 6.5, or between 5 and 6. In some embodiments, the pH of the antibody formulation is 5.0. In some embodiments, the pH of the antibody formulation is 6.0. In some embodiments, the pH of the antibody formulation is 7.0. Various means may be used to achieve the desired pH level, including, but not limited to, the addition of a suitable buffer. Other components may be included in the antibody formulation. In some embodiments, the antibody formulation may comprise a buffer (e.g., a histidine acetate, phosphate, or citrate buffer), a surfactant (e.g., polysorbate), and / or a stabilizing agent (e.g., human albumin), etc. In some embodiments, the antibody formulation may comprise pharmaceutically acceptable carriers, including, for example,Ion exchangers, alumina, aluminum stearate, lecithin, serum proteins such as human serum albumin, buffering agents such as phosphates, sucrose, glycine, sorbic acid, potassium sorbate, mixtures consisting of partial glycerides of saturated vegetable fatty acids, water, salts or electrolytes such as protamine sulfate, disodium hydrogen phosphate, potassium hydrogen phosphate, sodium chloride, zinc salts, colloidal silica, magnesium trisilicate, polyvinylpyrrolidone, cellulose-based substances, polyethylene glycol, sodium carboxymethylcellulose, polyacrylates, polyethylene-polyoxypropylene block polymers, and polyethylene glycol. In some embodiments, the antibody formulation further comprises a surfactant. In some embodiments, the surfactant is selected from the group consisting of polysorbate, sodium dodecyl sulfate, and nonionic surfactant. In some forms, the surfactant is polysorbate 20, i.e., polyoxyethylene (20)-sorbitan monolaurate, as represented by the formula: C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ Polysorbate 20 (PS-20) is commercially available from several suppliers, for example, Alkest® TW 20 (Oxiteno, Brazil) and Tween® 20 (Pierce, Rockford, IL). Applicants have found that by carefully controlling the concentration of PS-20 in the antibody formulation, the antibody has added stability and reduced particle formation when stored for extended periods. In some modes, PS-20 is approximately 0.001% to approximately 0.02%, of approximately a 0.002% to approximately 0.015%, of approximately a 0.002% to approximately 0.01%, of approximately a 0.004% to approximately 0.009%, of approximately a 0.005% to approximately 0.008%, approximately 0.007%, or approximately 0.006% of the antibody formulation. In some formulations, the antibody formulation also includes histidine. In some formulations, the antibody formulation comprises approximately 1 mM to approximately 100 mM, approximately 5 mM to approximately 80 mM of histidine, approximately 10 mM to approximately 60 mM of histidine, approximately 15 mM to approximately 50 mM of histidine, approximately 15 mM to approximately 30 mM of histidine, or approximately 20 mM histidine. In some formulations, several components of the antibody formulation may be omitted or the formulation may be substantially free of that component. The term "substantially free," as used herein, refers to an antibody formulation where the formulation contains less than 0.01%, less than 0.001%, less than 0.0005%, less than 0.0003%, or less than 0.0001% of the designated component. In some embodiments, the antibody formulation is substantially free of a saccharide; that is, the antibody formulation contains less than 0.01%, less than 0.001%, less than 0.0005%, less than 0.0003%, or less than 0.0001% of a saccharide. The term saccharide, as used herein, refers to a class of molecules that are derivatives of polyhydric alcohols. Saccharides are commonly called carbohydrates and can contain varying amounts of sugar (saccharide) units, e.g., monosaccharides, disaccharides, and polysaccharides. In some embodiments, the The C7QC Ln / Lznz / E / YILI formulation is substantially free of disaccharide. In some embodiments, the formulation is substantially free of a reducing sugar, a non-reducing sugar, or a sugar alcohol. In some embodiments, the antibody formulation is substantially free of proline, glutamate, sorbitol, divalent metal ions, and / or succinate. In some embodiments, the invention relates to a stable, aqueous antibody formulation comprising: (a) from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) from approximately 0.002% to approximately 0.01% of polysorbate-20, (c) from approximately 40 mM to approximately 60 mM of trehalose, and (d) from approximately 110 to approximately 150 mM of histidine. In some forms, the formulation also includes approximately 20 mM of histidine.In one embodiment, the invention relates to a stable, aqueous antibody formulation comprising: (a) from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.006% polysorbate-20, (c) approximately 50 mM trehalose, (d) approximately 130 mM L-arginine, and (e) approximately 20 mM histidine. In some embodiments, the invention relates to a stable, aqueous antibody formulation comprising: (a) from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) from approximately 0.002% to approximately 0.01% of polysorbate-20, (c) from approximately 200 mM to approximately 300 mM of trehalose, and (d) approximately 20 mM of histidine.In one embodiment, the invention relates to a stable, aqueous antibody formulation comprising: (a) from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.006% polysorbate-20, (c) approximately 250 mM trehalose, and (d) approximately 20 mM histidine.In another embodiment, the invention relates to a stable, aqueous antibody formulation comprising: (a) approximately 30 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, where the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and where the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, (b) approximately 0.006% polysorbate-20, (c) approximately 250 mM trehalose, and (d) approximately 20. C7QC Ln / ίΖΠΖ / Β / ΥΙΛΙ mM histidine. The antibody formulations of the present invention are an aqueous solution. In some embodiments, the antibody formulation has not been subjected to freezing temperatures and / or has not been frozen, i.e., it has been maintained in a liquid state. In some embodiments, the antibody in the antibody formulation has not been lyophilized. The term "stability," as used herein, generally refers to maintaining the integrity or minimizing the degradation, denaturation, aggregation, or unfolding of a biologically active agent such as a protein, peptide, or other bioactive macromolecule. The expression "enhanced stability," as used herein, generally refers to the fact that, under conditions known to cause degradation, denaturation, aggregation, or unfolding, the protein (e.g., an antibody such as an anti-IL5R antibody), peptide, or other bioactive macromolecule of interest maintains greater stability compared to a control protein, peptide, or other bioactive macromolecule. In some formulations, stability refers to an antibody formulation with low to undetectable levels of particle formation. C7QC Ln / I 7P7 / B / YILI, as used herein, refers to samples containing less than 30 particles / ml, less than 20 particles / ml, less than 20 particles / ml, less than 15 particles / ml, less than 10 particles / ml, less than 5 particles / ml, less than 2 particles / ml, or less than 1 particle / ml, as determined by HIAC analysis or visual examination. In some modalities, no particles are detected in the antibody formulation, either by HIAC analysis or visual examination. In some modalities, stability refers to reduced antibody fragmentation. The expression "low to undetectable levels of fragmentation," as used herein, refers to samples containing an amount equivalent to or greater than 80%, 85%, 90%, 95%, 98%, or 99% of the total protein, for example, in a single peak determined by HPSEC or in two peaks (e.g., light and heavy chains) (or as many peaks as there are subunits) by reduced capillary gel electrophoresis (rCGE), representing the undegraded antibody or an undegraded fragment thereof, and containing no other individual peaks containing more than 5%, 4%, 3%, 2%, 1%, or 0.5% of the total protein in each of them.The expression reduced gel capillary electrophoresis, as used herein, refers to gel capillary electrophoresis under reducing conditions sufficient to reduce disulfide bonds in an antibody. A person skilled in the art will appreciate that the stability of a protein depends on characteristics other than the formulation composition. For example, stability can be affected by temperature, pressure, humidity, pH, and external forms of radiation. Thus, unless otherwise specified, the stability referenced herein is considered to be measured at 5 °C, one atmosphere of pressure, 50% relative humidity, pH 6.0, and normal background radiation levels. The stability of the antibody in the antibody formulation can be determined using various methods. In some modalities, antibody stability is determined by size exclusion chromatography (SEC). SEC separates analytes (e.g., macromolecules such as proteins and antibodies) based on a combination of their hydrodynamic size, diffusion coefficient, and surface properties.Thus, for example, SEC can separate antibodies in their natural three-dimensional conformation from antibodies in various states of denaturation and / or antibodies that have been degraded. In SEC, the stationary phase is generally composed of inert particles packed in a dense three-dimensional matrix inside a glass or steel column. The mobile phase... The stationary phase can be pure water, an aqueous buffer, an organic solvent, mixtures of these, or other solvents. The stationary phase particles have small pores and / or channels that allow only species smaller than a certain size to enter. Consequently, large particles are excluded from these pores and channels, while smaller particles are removed from the mobile phase flow. The time particles remain immobilized in the stationary phase pores depends, in part, on the depth to which they have penetrated the pore. Their removal from the mobile phase flow causes their elution from the column to take longer, resulting in particle separation based on size differences. In some modalities, SEC is combined with an identification technique to identify or characterize proteins or protein fragments. Protein identification and characterization can be performed using various techniques, including, but not limited to, chromatographic techniques, e.g., high-performance liquid chromatography (HPLC), immunoassays, electrophoresis, ultraviolet / visible / infrared spectroscopy, Raman spectroscopy, surface-amplified Raman spectroscopy, mass spectrometry, gas chromatography, static light scattering (SLS), Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD), urea-induced protein unfolding techniques, tryptophan intrinsic fluorescence, differential scanning calorimetry, and / or protein binding to ANS. In some methods, protein identification is performed using high-performance liquid chromatography (HPLC). Experts in the technique are familiar with various instruments and apparatus for performing HPLC. Generally, HPLC involves introducing a liquid solvent containing the protein of interest into a separation column, where the separation takes place. The HPLC separation column is packed with solid particles (e.g., silica, polymers, or sorbents), and the sample mixture is separated into its constituent compounds as it interacts with the column particles. HPLC separation is affected by solvent conditions (e.g., pressure, temperature), chemical interactions between the sample mixture and the liquid solvent (e.g., hydrophobicity, protonation, etc.), and chemical interactions between the sample mixture and the solid particles packed within the separation column (e.g.,, ligand affinity, ion exchange, etc.) . In some modalities, SEC and protein identification take place in the same instrument or simultaneously. For example, SEC and HPLC can be combined, C7QC Ln / ίZΖΠZΖ / Β / YΙΛΙ which is often called SE-HPLC. In some embodiments, the aqueous formulation comprises from approximately 2 mg / ml to approximately 100 mg / ml of antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the formulation is stable after storage at approximately 40°C for at least 1 month. In some embodiments, the formulation is stable after storage at approximately 25°C for at least 3 months. In some embodiments, the formulation is stable after storage at approximately 5°C for at least 6 months.In some formulations, the formulation is stable after storage at approximately 5°C for at least 12 months. In some formulations, the formulation is stable after storage at approximately 5°C for at least 18 months. In some formulations, the formulation is stable after storage at approximately 5°C for at least 24 months, or 36 months. The term "stable" can be relative rather than absolute. Therefore, in some formulations, an antibody is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 2°C to 8°C for 6 months. In some formulations, an antibody is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 2°C to 8°C for 12 months.In some formulations, the antibody in the antibody formulation is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 2°C to 8°C for 18 months. In some formulations, the antibody in the antibody formulation is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 2°C to 8°C for 24 months. In some formulations, the antibody is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 23°C to 27°C for 3 months. In some formulations, the antibody is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 23°C to 27°C for 6 months.In some formulations, the antibody is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 23°C to 27°C for 12 months. In some formulations, the antibody is considered stable if less than 20%, 15%, 10%, 5%, or 2% of the antibody degrades, denatures, aggregates, or unfolds, as determined by SEC HPLC, when the antibody is stored at 23°C to 27°C for 24 months. In some modalities, the antibody is stable if less than 6%, less than 4%, less than 3%, less than 2% or less than 1% of the antibody degrades, denatures, aggregates, or unfolds per month, as determined by SEC HPLC, when the antibody is stored at 40°C. In some modalities, the antibody is stable if less than 6%, less than 4%, less than 3%, less than 2%, or less than 1% of the antibody degrades, denatures, aggregates, or unfolds per month, as determined by SEC HPLC, when the antibody is stored at 5°C. In some embodiments, the antibody formulations of the present invention may be considered stable if the antibody exhibits very little or no loss of antibody-binding activity (including its antibody fragments) of the formulation compared to a reference antibody, as measured by antibody-binding assays known to those skilled in the art, such as ELISA, etc., over a period of 8 weeks, 4 months, 6 months, 9 months, 12 months, or 24 months. In some embodiments, the antibody stored at approximately 40°C for at least 1 month retains at least 80%, at least approximately 85%, at least approximately 90%, at least approximately 95%, at least approximately 98%, or at least approximately 99% of the IL-5 receptor polypeptide-binding capacity compared to a reference antibody that has not been stored.In some formulations, the antibody stored at approximately 5°C for at least 6 months retains at least 80%, at least approximately 85%, at least approximately 90%, at least approximately 95%, at least approximately 98%, or at least approximately 99% of the binding capacity to an IL-5 receptor polypeptide compared to an unstored reference antibody. In some formulations, the antibody stored at approximately 40°C for at least 1 month retains at least 95% of the binding capacity to an IL-5 receptor polypeptide compared to an unstored reference antibody. In some formulations, the antibody stored at approximately 5°C for at least 6 months retains at least 95% of the binding capacity to an IL-5 receptor polypeptide compared to an unstored reference antibody. Antibody formulations can provide low to undetectable levels of antibody aggregation. The expression "low to undetectable levels of aggregation," as used herein, refers to samples containing no more than approximately 5%, no more than approximately 4%, no more than approximately 3%, no more than approximately 2%, no more than approximately 1%, and no more than approximately 0.5% of protein aggregation by weight, as measured. C7QC Lh / ίZРZ / B / YILI using high-performance size exclusion chromatography (HPSEC) or static light scattering (SLS). In some formulations, less than 2% of the antibody forms an aggregate after storage at approximately 40°C for at least 4 weeks, as determined by HPSEC. In some formulations, less than 2% of the antibody forms an aggregate after storage at approximately 5°C for at least 3 months, at least 6 months, at least 9 months, at least 12 months, at least 15 months, at least 18 months, at least 24 months, or at least 36 months, as determined by HPSEC. Applicants have found that the antibody formulations provided herein result in greatly reduced particle formation, as determined by visual inspection, microflow imaging (MFI), or size exclusion chromatography (SEC). In some embodiments, the formulation is substantially particle-free after storage at approximately 40°C for at least 1 month, as determined by visual inspection. In some embodiments, the formulation is substantially particle-free after storage at approximately 5°C for at least 6 months, at least 9 months, at least 12 months, at least 15 months, at least 18 months, at least 24 months, or at least 36 months, as determined by visual inspection. In some embodiments, the antibody formulation of the present invention can be used for pharmaceutical purposes. Antibodies used in pharmaceutical applications generally need to exhibit a high level of purity, particularly with regard to cell culture contaminants, including cellular protein contaminants, cellular DNA contaminants, viruses, and other transmissible agents. Refer to WHO Requirements for the use of animal cells as in vitro substrates for the production of biologicals: Requirements for Biological Substances No. 50, No. 878, Annex 1, 1998. In response to concerns about contaminants, the World Health Organization (WHO) has established limits on the levels of several contaminants. For example, the WHO recommends a DNA limit of less than 10 ng per dose for protein products.Similarly, the U.S. Food and Drug Administration (FDA) has set a DNA limit of 0.5 pg / mg of protein or less. Thus, in some embodiments, the present invention relates to antibody formulations that exceed or meet the limits for contaminants defined by one or more governmental organizations, e.g., the U.S. Food and Drug Administration and / or the World Health Organization. In some modalities, the formulation of antibodies The C7QC Ln / įZРZ / B / YILI described herein is pharmaceutically acceptable. The term "pharmaceutically acceptable" refers to an antibody formulation that is, in the opinion of a physician, suitable for contact with human and animal tissues without causing excessive toxicity or other complications, and with a reasonable benefit-risk ratio. The purity of antibody formulations may vary. In some modalities, the therapeutic antibody of interest, e.g., the anti-IL5R antibody, represents more than 90% (w / w) of the total polypeptides present in antibody formation. In some modalities, the therapeutic antibody of interest, e.g., anti-IL5R, represents more than 95% (w / w), 98% (w / w), 99% (w / w), 99.5% (w / w), or 99.9% (w / w) of the total polypeptide present in antibody formation. The formulations as provided herein may be suitable for the treatment of a subject. The term subject, as used herein, may be used interchangeably with patient and refers to any animal classified as a mammal, including humans and non-humans such as, without limitation, farm and domestic animals, zoo animals, animals participating in sports, and pets. In some modalities, the subject refers to a human being. The terms "treat" and "treatment" refer to both therapeutic treatment and prophylactic, maintenance, or preventive measures, where the objective is to prevent or alleviate (mitigate) an unwanted physiological condition, disorder, or disease, or to obtain desired or beneficial clinical results. The terms "treat," "treatment," and "that treats" refer to the reduction or improvement of the course, severity, and / or duration of such a disease or disorder (e.g.,A disease or disorder characterized by abnormal activity and / or expression of an IL5-like polypeptide, an autoimmune disease, an inflammatory disease, a proliferative disease, or an infection, or the improvement of one or more of its symptoms, as a result of the administration of one or more therapies (including, but not limited to, the administration of one or more therapeutic or prophylactic agents). In certain modalities, such terms refer to a reduction in inflammation mediated by eosinophils associated with inflammation. In other modalities, such terms refer to a reduction in the release of inflammatory agents by mast cells or a reduction in the biological effect of such inflammatory agents.In other modalities, these terms refer to a reduction in the growth, formation, and / or increase in the number of hyperproliferative cells (e.g., cancer cells). In still other modalities, these terms refer to a reduction in inflammation of the airways, skin, gastrointestinal tract, or combinations thereof. In yet other modalities, these terms refer to a reduction in symptoms associated with asthma. In some modalities, these terms refer to a reduction in symptoms associated with chronic obstructive pulmonary disease (COPD). The antibody formulation of the present invention can be administered to a subject by various means. In some embodiments, the antibody formulation is suitable for parenteral administration, for example, by inhalation (e.g., aerosol spray or powder), transmucosal, intravenous, subcutaneous, or intramuscular administration. In some embodiments, the formulation is an injectable formulation. In some embodiments, the invention relates to a sealed container comprising any of the antibody formulations as described herein. In some respects, the present invention relates to various pharmaceutical dosage forms. Various dosage forms could be applied to the formulations provided herein. See, for example, Pharmaceutical Dosage Form: Parenteral Medications, volume C70C Ln / ί7Π7 / E / YΙΛΙ 1, 2nd edition. In one embodiment, a pharmaceutical unit dosage of the invention comprises an antibody formulation in a suitable container, for example, a vial or syringe. In one embodiment, a pharmaceutical unit dosage of the invention comprises an antibody formulation administered intravenously, subcutaneously, or intramuscularly. In another embodiment, a pharmaceutical unit dosage of the invention comprises an antibody formulation administered by aerosol. In one specific embodiment, a pharmaceutical unit dosage of the invention comprises an antibody formulation administered subcutaneously. In another embodiment, a pharmaceutical unit dosage of the invention comprises an antibody formulation administered by aerosol. In a further embodiment, the pharmaceutical unit dosage of the invention comprises an antibody formulation administered intranasally. The antibody formulations of the present invention can be prepared as unit-dose forms by preparing a vial containing an aliquot of the aqueous antibody formulation for single use. For example, a unit-dose vial may contain 1 ml, 2 ml, 3 ml, 4 ml, 5 ml, 6 ml, 7 ml, 8 ml, 9 ml, 10 ml, 15 ml, or 20 ml of different concentrations of an antibody. C7QC Ln / ίZЖРZ / B / YILI antibody that specifically binds to the IL5 receptor ranges from approximately 0.1 mg / ml to approximately 300 mg / ml. If necessary, these preparations can be adjusted to a desired concentration by adding a sterile diluent to each vial. In one specific embodiment, the aqueous antibody formulations of the present invention are formulated in single-dose vials as a sterile liquid containing from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 8-10, of approximately 0.0.02% to approximately 0.01% of polysorbate-20, from approximately 40 mM to approximately 60 mM of trehalose, and from approximately 110 mM to approximately 150 mM of L-arginine. In another specific embodiment, the aqueous antibody formulations of the present invention are formulated in single-dose vials as a sterile liquid containing from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a chain variable region. C70C Ln / ί7P7 / E / YILI light, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, from approximately 0.002% to approximately 0.01% polysorbate-20, and from approximately 200 mM to approximately 300 mM trehalose. In one embodiment, the antibody of the invention is supplied at 2 to 20 mg / mL in 3 cc amber borosilicate type I vials of the USP (West Pharmaceutical Services Part No. 6800-0675). In another embodiment, the antibody of the invention is supplied at 20 to 100 mg / ml in 3 cc amber borosilicate type I vials of the USP. The target fill volume is 1.2 ml. The antibody formulations of the present invention can be prepared as unit-dose forms by preparing a pre-filled syringe containing an aliquot of the aqueous antibody formulation for single use. For example, a unit-dose pre-filled syringe may contain 0.1 ml, 0.2 ml, 0.3 ml, 0.4 ml, 0.5 ml, 0.6 ml, 0.7 ml, 0.8 ml, 0.9 ml, 1 ml, 2 ml, 3 ml, 4 ml, 5 ml, 6 ml, 7 ml, 8 ml, 9 ml, 10 ml, 15 ml, or 20 ml of different concentrations of an antibody that specifically binds to an IL-5 polypeptide, ranging between C70C Ln / ί7Π7 / Ε / ΥΙΛΙ approximately 2 mg / ml and approximately 100 mg / ml. In one specific embodiment, the aqueous antibody formulations of the present invention are formulated in single-dose pre-filled syringes as a sterile liquid containing from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, from approximately 0.002% to approximately 0.01% of polysorbate-20, from approximately 40 mM to approximately 60 mM of trehalose, and from approximately 110 mM to approximately 150 mM of L-arginine.In one specific embodiment, the aqueous antibody formulations of the present invention are formulated in single-dose pre-filled syringes as a sterile liquid containing from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, from approximately 0.002% to approximately 0.01% of polysorbate-20, and from approximately 200 mM to approximately 300 mM of trehalose. Various dosage amounts can be administered in a single use. For example, some formulations may contain 0.1 mg, 0.2 mg, 0.3 mg, 0.4 mg, 0.5 mg, 0.6 mg, 0.7 mg, 0.8 mg, 0.9 mg, 1.0 mg, 1.1 mg, 1.2 mg, 1.3 mg, 1.4 mg, 1.5 mg, 1.6 mg, 1.7 mg, 1.8 mg, 1.9 mg, 2 mg, 3 mg, 4 mg, 5 mg, 6 mg, 7 mg, 8 mg, 9 mg, 10 mg, 12 mg, 14 mg, 16 mg, 18 mg, 20 mg, 30 mg, 40 mg, 50 mg, 70 mg, or 100 mg of antibody in a single dose. Various types of syringes can be used. The syringe can be filled with the antibody formulation immediately before administration to a subject, for example, less than 1 week, 1 day, 6 hours, 3 hours, 2 hours, 1 hour, 30 minutes, 20 minutes, or 10 minutes before administration. In some modalities, the syringe is filled with the antibody formulation at the point of sale or by the treatment center. In some modalities, the syringe is pre-filled, for example, more than 1 day, 2 days, 4 days, or 1 C70C Ln / ί7Π7 / E / YΙΛΙ week, 2 weeks, 1 month, 2 months, 3 months, 6 months, 12 months, 18 months, 24 months, 3 years or 4 years prior to administration to a subject. In some embodiments, the pre-filled syringe comprises a needle, for example, a 27G regular wall needle, a 27G thin wall needle, a 29G regular wall needle or a 29G thin wall needle. In some embodiments, the pre-filled syringe comprises a 29G thin wall needle. In some embodiments, any syringe suitable for administration to the intended subject may be used. In some embodiments, the syringe is a plastic syringe or a glass syringe. In some embodiments, the syringe is made of materials that are substantially tungsten-free. In some embodiments, the syringe is coated with silicone. In some embodiments, the pre-filled syringe comprises a plunger that has a fluoropolymer resin disc. Examples of syringes may include, but are not limited to, Biotech Hypak™ syringes 1 ml in length (Becton Dickinson), with a 1 ml plunger cap Hypak from Becton Dickinson 4023 Flurotec Daikyo SilOOO (Catalog No. 47271919), C3Pin (Lot No. E912701), Biotech Hypak™ with 0.8 mg of silicone oil (Becton Dickinson) and CZ (West, Catalog No. 19550807). The aqueous antibody formulations of the present invention can be sterilized by various sterilization methods, including sterile filtration, radiation, etc. In one specific embodiment, the diafiltered antibody formulation is sterilized by filtration through a pre-sterilized 0.2-micrometer filter. Sterilized antibody formulations of the present invention can be administered to a subject to prevent, treat, and / or manage an immune response, such as an inflammatory response. In some embodiments, the prefilled syringe comprises (a) approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and (b) approximately 0.002% to approximately 0.01% of polysorbate-20. In some embodiments, the prefilled syringe further comprises (c) approximately 40 mM to approximately 60 mM of trehalose, and (d) approximately 110 mM to approximately 150 mM of L-arginine.In some embodiments, the prefilled syringe comprises (a) approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and (b) approximately 0.002% to approximately 0.01% of polysorbate-20. In some embodiments, the prefilled syringe further comprises (c) approximately 200 mM to approximately 300 mM of trehalose. In some embodiments, the invention relates to a kit comprising any of the antibody formulations described herein, the containers described herein, the unit dosage forms described herein, or the pre-filled syringe described herein. In some embodiments, the present invention may also relate to a method of producing a stable, aqueous antibody formulation comprising an antibody, the method comprising: (a) purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the numbering system of C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ Kabat of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; and (b) placing the isolated antibody in a stabilization formulation to form a stable, aqueous antibody formulation, wherein the resulting stable, aqueous antibody formulation comprises: (i) from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and (ii) from approximately 0.002% to approximately 0.01% of polysorbate-20.In some embodiments, the invention relates to a method of preparing a stable, aqueous antibody formulation, the method comprising: (a) purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO:. 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; (b) diluting the antibody to approximately 2 mg / ml to approximately 20 mg / ml, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 8-10, to give a solution comprising: (i) approximately 0.002% to approximately 0.01% polysorbate-20, (ii) approximately 40 mM to approximately 60 mM trehalose, and (iii) approximately 110 mM to approximately 150 mM L-arginine. In some embodiments,The invention relates to a method for preparing a stable, aqueous antibody formulation, the method comprising: (a) purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy chain variable region and a light chain variable region, where the heavy chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 5-7, and where the light chain variable region comprises the CDR1, CDR2, and CDR3 sequences according to the Kabat numbering system of SEQ ID NO: 8-10; (b) diluting the antibody from approximately 20 mg / ml to approximately 100 mg / ml, wherein the antibody comprises a heavy chain variable region and a light chain variable region, where the heavy chain variable region comprises the CDR1 sequence,CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, to give a solution comprising: (i) from about 0.002% to about 0.01% polysorbate-20, (ii) from about 200 mM to about 300 mM trehalose and (iii) about 20 mM histidine. Although many aspects of the invention relate to aqueous formulations, it should be noted for the purposes of equivalents that the antibodies or antibody formulations of the invention can be lyophilized if desired. The invention therefore encompasses lyophilized forms of the formulations of the invention, or lyophilized antibodies that are subsequently reconstituted in an aqueous form. In some embodiments, the invention relates to a method of producing a reconstituted antibody formulation comprising a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, the method comprising: (a) purifying the antibody from a cell culture;(b) lyophilizing the isolated antibody; (c) adding the lyophilized antibody to an aqueous solution to form a reconstituted antibody formulation, wherein the reconstituted antibody formulation comprises: (i) from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and (ii) from approximately 0.002% to approximately 0.01% of polysorbate-20. In some embodiments, the inventors have found that anti-IL5R antibody formulations with reduced glutathione S-transferase (GST) concentrations result in reduced (e.g., undetectable) particle formation. Particle removal is important to avoid potential immunogenicity and limit the impact on product quality. In some embodiments, GST concentrations are reduced using affinity chromatography. In some embodiments, GST concentrations are reduced using a protein A column. In some embodiments, the protein A column is MabSelect Sure (GE Healthcare Life Sciences). In some embodiments, GST concentrations are reduced using mixed-mode chromatography. In some embodiments, the mixed-mode column is Capto™ Adhere (GE Healthcare Life Sciences). In some embodiments, the invention relates to an antibody formulation comprising an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially particle-free. In some embodiments, the term essentially particle-free refers to the C7QC Lh / ίZРZ / B / YILI absence of visible particles when observed under an illumination box. In some modalities, the term essentially particle-free is synonymous with the expression low to undetectable levels of particle formation as described above. In some modalities, essentially particle-free refers to samples containing less than 30 particles / ml, less than 20 particles / ml, less than 20 particles / ml, less than 15 particles / ml, less than 10 particles / ml, less than 5 particles / ml, less than 2 particles / ml, or less than 1 particle / ml where the particles are larger than 25 pm and the particle count is determined by HIAC analysis or visual analysis.In some modalities, essentially particle-free refers to samples containing 1 to 50 particles / ml, 2 to 40 particles / ml, 3 to 30 particles / ml, 4 to 25 particles / ml, or 5 to 20 particles / ml where the particles are larger than 25 µm and the particle count is determined by HIAC analysis or visual analysis. In some modalities, the term visible particles refers to particles larger than 25 µm. In some modalities, essentially particle-free refers to samples containing 1 to 200 particles / ml, 10 to 150 particles / ml, 30-100 particles / ml or 40 to 80 particles / ml in which the C7QC Ln / I 7P7 / B / YILI particles are larger than 5 pm and the particle count is determined by HIAC analysis or visual examination. In some modalities, the term visible particles refers to particles larger than 5 pm. In some modalities, no particles are detected in the antibody formulation, either by HIAC analysis or visual examination. In some embodiments, the invention relates to an antibody formulation comprising an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially free of glutathione S-transferase (GST). Unless otherwise specified, the term essentially free of glutathione S-transferase or essentially free of GST would encompass a composition lacking active GST (but which may contain inactive GST) as well as a composition that does not have the GST protein, in either its active or inactive form.In some embodiments, the invention relates to an antibody formulation comprising an antibody. C7QC Ln / Lznz / E / YILI wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially free of active GST. The term active GST refers to GST that can catalyze the formation of the thiol group of glutathione (GSH) with an electrophilic compound such as 1-chloro-2,4-dinitrobenzene (CDNB) to form a GS-DNB conjugate.GST, or glutathione S-transferase, refers to a family of enzymes that can catalyze numerous reactions, but primarily the conjugation of reduced glutathione, via a sulfhydryl group, with electrophilic centers, such as aromatic compounds, double bonds, C-C1X, etc. GST monomers are generally in the 22–29 kDa range, but can also occur as dimers, trimers, and heterodimers (with other proteins). In some formulations, the term GST refers to a protein that can catalyze the formation of the thiol group of glutathione (GSH) with 1-chloro-2,4-dinitrobenzene (CDNB) to form a GS-DNB conjugate. In some embodiments, the invention relates to an antibody formulation comprising an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially particle-free for at least 1 month, at least 2 months, at least 3 months, at least 4 months, at least 5 months, at least 6 months, at least 8 months, at least 10 months, at least 12 months, or at least 18 months when stored at 38-42°C.In some embodiments, the invention relates to an antibody formulation comprising an antibody in which the antibody comprises a heavy chain variable region and a light chain variable region, in which the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and in which the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, in which the antibody formulation is essentially particle-free for at least 1 month, at least 2 months, at least 3 months, at least 4 months, at least 5 months. C70C Ln / ί7Π7 / E / YΙΛΙ months, at least 6 months, at least 8 months, at least 10 months, at least 12 months, at least 18 months, at least 24 months, at least 30 months, at least 36 months or at least 48 months when stored at 2-6° C. In some formulations, the antibody formulation is essentially GST-free. In some formulations, the term essentially GST-free refers to an antibody formulation that has a GST activity of less than approximately 0.5 units / mg of antibody. of approximately 0.3 units / mg of antibody, less than approximately 0.1 units / mg of antibody, less than approximately 0.08 units / mg of antibody, less than approximately 0.05 units / mg of antibody, less than approximately 0.03 units / mg of antibody, less than approximately 0.01 units / mg of antibody, less than approximately 0.005 units / mg of antibody, less than approximately 0.001 units / mg of antibody, less than approximately 5 x 10⁻³ units / mg of antibody, less than approximately 1 x 10⁻⁴ units / mg of antibody, less than approximately 1 x 10⁻⁵ units / mg of antibody, or less than approximately 1 x 10⁻¹ units / mg of antibody. In some modalities, the term essentially free refers to a GST level that is not detectable using common GST detection techniques. Experts in the technique are familiar with various methods for determining GST activity. In some modalities, GST activity is determined using a fluorometric glutathione assay kit (GSH / GSSG / Total) (BioVision, San Francisco, CA). In some embodiments, the invention relates to a method for purifying an antibody comprising a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, the method comprising (i) obtaining a cell culture comprising the antibody, (ii) performing affinity chromatography on the antibody, (iv) performing cation exchange on the antibody, and (v) performing mixed-mode chromatography on the antibody.In some embodiments, the invention relates to a method for purifying an antibody, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, the method comprising (i) obtaining a cell culture comprising the antibody, (ii) attaching the antibody to a protein A column, (iii) eluting the antibody from the protein A column, (iv) performing cation exchange on the antibody, and (v) performing mixed-mode chromatography on the antibody. In some embodiments, the antibody purification method further comprises a viral inactivation process.In some methods, the virus inactivation step is performed by lowering the pH to below 4.0. In some methods, the process also includes diafiltration. In some methods, the process also includes filtration. In some methods, filtration alone is sufficient to remove active virus particles. In some embodiments, the invention relates to a method of treating a patient. In some embodiments, the method comprises administering the antibody formulations described herein, the containers described herein, the unit-dose forms described herein, or the pre-filled syringe described herein to a subject in need. In some embodiments, the invention is suitable for the treatment of pulmonary disease or disorder by administering the antibody formulation described herein. C7QC Ln / įZРZ / B / YILI In some embodiments, the invention relates to a method for treating a patient with an eosinophilic disease or disorder by administering the antibody formulation described herein. In some embodiments, the invention relates to a method for treating a pulmonary disease or disorder in a subject, wherein the method comprises administering the antibody formulations described herein. In some embodiments, the invention relates to a method for treating an eosinophilic disease or disorder in a subject, wherein the method comprises administering the antibody formulations described herein.In some embodiments, the invention relates to the treatment of pulmonary diseases or disorders, for example, asthma, COPD, eosinophilic asthma, combined eosinophilic and neutrophilic asthma, aspirin-responsive asthma, allergic bronchopulmonary aspergillosis, acute and chronic eosinophilic bronchitis, acute and chronic eosinophilic pneumonia, Churg-Strauss syndrome, hypereosinophilic syndrome, pulmonary eosinophilia induced by drugs, irritants, and radiation, pulmonary eosinophilia induced by infection (fungi, tuberculosis, parasites), autoimmune-related pulmonary eosinophilia, eosinophilic esophagitis, or Crohn's disease, or a combination thereof, in a subject, the method comprising administering the antibody formulations described herein. In some embodiments, the invention relates to the treatment of asthma in a subject, wherein the method comprises administering the antibody formulations described herein.In some embodiments, the invention relates to the treatment of COPD in a subject, where the method comprises administering the antibody formulations described herein. In some modalities, a therapeutically effective amount of the antibody formulations described herein is administered to treat a condition. The term therapeutically effective amount, as used herein, refers to the amount of a therapy (e.g., an antibody that binds immunospecifically to an IL5-like polypeptide) that is sufficient to reduce the severity of a disease or disorder (e.g.,, a disease or disorder characterized by abnormal activity and / or expression of an IL5-type polypeptide, a disease or disorder characterized by abnormal activity and / or expression of an IL5 receptor or one or more subunits thereof, an autoimmune disease, an inflammatory disease, a proliferative disease or an infection (preferably a respiratory infection) or one or more of its symptoms), reduce the duration of a respiratory condition, improve one or more symptoms of such a disease or disorder, prevent the progression of such a disease or disorder. C7QC Ln / I 7P7 / B / YILI to cause the regression of such a disease or disorder, or to potentiate or enhance the therapeutic effects of another therapy. In some modalities, the therapeutically effective amount cannot be specified in advance and may be determined by a caregiver, for example, a physician or other healthcare professional, using various means, for example, dose titration. Appropriate therapeutically effective amounts may also be determined by routine experimentation using, for example, animal models. The terms therapies and therapy may refer to any protocols, methods, and / or agents that can be used in the prevention, treatment, management, or improvement of a disease or disorder (e.g., a disease or disorder characterized by abnormal activity and / or expression of an IL5-like polypeptide, a disease or disorder characterized by abnormal activity and / or expression of an IL5 receptor or one or more of its subunits, an autoimmune disease, an inflammatory disease, a proliferative disease, or an infection (preferably a respiratory infection) or one or more of its symptoms). In certain modalities, the terms therapy and therapy refer to a biologic therapy, supportive therapy, and / or other therapies useful in the treatment, management, prevention, or improvement of such a disease or disorder. C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ disorder or one or more symptoms known to expert medical personnel. The term therapeutic protocol, as used herein, refers to a regimen for dosing and scheduling the administration of one or more therapies (e.g., therapeutic agents) that exhibits therapeutic efficacy. The antibody formulation of the present invention may be administered by, for example, oral, parenteral, inhalation, or topical routes. The term parenteral, as used herein, includes, for example, intravenous, intra-arterial, intraperitoneal, intramuscular, subcutaneous, rectal, or vaginal administration. In some embodiments, the antibody is an anti-IL5R antibody, and the route of administration is intramuscular injection. Although it is clearly contemplated that all these forms of administration are within the scope of the invention, in some embodiments, the antibody formulation is suitable for administration by injection, particularly by drip or intra-arterial or intravenous injection. In some embodiments, the compositions and methods of the present invention enable a manufacturer to produce an antibody formulation suitable for administration to a human being more efficiently, either by reducing costs, reducing steps in the method, reducing opportunities for error, reducing opportunities to introduce unsuitable or unsafe additives, reducing waste, increasing storage time, etc. EXAMPLES Example 1 Formulation studies were conducted to develop a stable anti-IL5R antibody formulation suitable for subcutaneous administration of 2–100 mg doses from a pre-filled syringe (or an inverted vial). Specifically, two antibody concentration-independent formulations were developed: a 2–20 mg / mL formulation and a 20–100 mg / mL formulation. 1. Materials and methods a. Source of anti-IL5R antibody and preparation of formulations Multiple lots of anti-IL5R antibody were used in these studies. All lots were produced at various scales by MedImmune and dispensed after diafiltration and concentration to approximately 130 g / L in 20 mM histidine / histidine HCl at pH 6. The same lots also contained 250 mM trehalose in the diafiltration buffer. Anti-IL5R antibody was formulated by performing known additions in excipient addition buffer (EAB) to achieve an anti-IL5R antibody concentration of 100 g / 1 and C7QC Ln / įZРZ / B / YILI appropriate concentrations of buffer species and excipient. Lower concentration pharmacological substances were prepared from the 100 g / 1 formulation. 2. Accelerated stress methods a. Storage at elevated temperature Vials and syringes were stored in controlled stability chambers to maintain a constant temperature during storage. The chambers were maintained at 2–8°C, 23–27°C / 60% RH, or 38–42°C / 75% RH, but will be referred to by their midpoint temperatures of 5°C, 25°C, or 40°C hereafter. Vials were stored upright unless otherwise specified, and pre-filled syringes were stored with the tip pointing downwards. b. Freeze-thaw cycles Both controlled and uncontrolled freeze-thaw cycles were used in these studies. Uncontrolled freeze-thaw cycles were performed by freezing the vials in a -40°C chamber and thawing them at room temperature. c. Transport and agitation A variety of methods were used to investigate the effect of transport on the anti-IL5R antibody. Vials were shaken on a workbench using orbital shaking at 150 rpm for 24 hours. Actual transport was simulated by sending the product to an external location. The C70C Ln / ί7Π7 / E / YΙΛΙ product made two round trips and was transported by air and land over 4 days. A combination of frozen and chilled packages was used to maintain the product temperature at 2-8°C, and it was monitored by sensors that indicated temperatures below 0°C or above 9°C. For selection studies, transport was simulated using a vibration table (transport simulator). The product was subjected to air and ground transport in a pattern similar to that experienced during a round-trip shipment. The process lasted 12 hours, and the temperature was again controlled with cold packs to maintain 2–8°C; no sensors were used. Horizontal orientation was chosen as the worst-case orientation during actual or simulated shipping due to the potential for bubble formation during transit and the possibility of the drug coming into contact with the entire barrel, needle tip, and cap. 3. Experimental methods a. Methods that follow or are derived from a SOP Visual inspections were performed, comparing with particle and opalescence patterns. Aggregation and fragmentation were monitored by SE-HPLC. For anti-IL5R antibody concentrations below 10 g / L, a larger injection volume was used to achieve a mass of C7QC Ln / ίZΖΠZ / Β / YILI total protein similar by injection. Some samples were also used for cIEF and RP-HPLC measurements to monitor fragmentation. b. Protein concentration The protein concentration was measured by diluting the protein using serial gravimetric dilution to approximately 0.5 g / L and measuring the absorbance at 280 nm. The concentration was calculated from the extinction coefficient and the dilution factor, and corrected for the density effect in gravimetric dilution for initial concentrations above 50 g / L. c. Subvisible particle count Subvisible particle counts were performed using both MFI and HIAC. For MFI, 0.9 mL of solution was processed neat after optical illumination was treated with water. The first 0.2 mL were used to purge the system and were not included in the analysis. An aspect ratio filter of <0.85 was used to remove spherical air bubbles or silicone oil droplets. For HIAC, solutions with concentrations >5 g / L were diluted to approximately 5 g / L, while diluted samples were processed neat. Dilution was performed in a laminar flow hood using 20 mM, pH 6, histidine / histidine HCl buffer, which was filtered immediately before use. Samples were degassed under vacuum for at least 30 minutes. C70C Ln / ί7Π7 / E / YILI minutes before testing. The average of three runs was multiplied by the dilution factor to obtain the final result. Silicone oil droplets were indistinguishable from protein particles by HIAC. 4. Data and discussion a. Examination of the concentration of polysorbate-20 The first objective was to optimize the concentration of PS20 in the aqueous antibody formulation. Polysorbate was included in the solutions to protect the protein from denaturation and aggregation at contact surfaces, and it was determined that the required concentration would differ in the liquid product compared to the lyophilized product. The main interfacial tensions were encountered during freeze-thaw and transport, so the experimental design focused on mimicking these stresses. Previous experience indicated that 0.02% polysorbate 20 was sufficient to provide complete protection against both of these stresses (data not shown). As a verification, these stresses were combined sequentially, in the order expected for clinical production, and an incubation period was added after each stress to allow for the growth of any potential particles.First, the drug substance was subjected to three uncontrolled freeze-thaw cycles, and the material was filtered and loaded into vials. These were then shaken on the workbench and incubated for one week. The sample was heated to 40°C before testing by SE-HPLC and MFI. The test conditions were the extremes of the concentration range, 2 and 100 g / L, formulated in 240 mM trehalose, 20 mM histidine / histidine HCl, pH 6 with varying PS-20 levels of 0-0.03% w / v. The results are shown in Figures 2, 3, and 4. Monomer fraction data indicated that the 2 g / L solution remained pure regardless of the polysorbate level, but that low amounts of polysorbate-20, below approximately 0.005%, caused a small amount of aggregation at 100 g / L. However, these results alone did not indicate that the solution was on the verge of failure. The stresses used were intense, and the level of degradation minimal; therefore, any PS20 level tested could be adequate from an SEC aggregation perspective. At 2 g / L, subvisible particle counts were quite high and were not controlled by polysorbate-20 in the tested range. At 100 g / L, high subvisible particle counts were controlled by the presence of 0.003% or more PS20. Taken together, these data indicated that PS20 levels should be kept at or above 0.003%. An alternative method of controlling subvisible particles for low concentration solutions was required, as discussed below. b. pH test The effect of solution pH was studied in 2, 20, and 100 g / L solutions with pH values ​​ranging from 5 to 7.5. The rest of the formulation was kept constant and included 240 mM trehalose, 20 mM histidine / histidine-HCl, and 0.02% PS-20. Solutions were prepared and stored at 40°C for one month prior to testing. Monomer loss was assessed for all samples by SE-HPLC, subvisible particles by MFI, and visible particles by visual inspection. Additional tests were performed on the 100 g / L samples, including RP-HPLC and cIEF. The results are presented in Figures 5 and 6. Aggregation and fragmentation were minimized within the pH range of 5.5–6.5. cIEF results were consistent with the reference standard at pH 7.0 and above. Subvisible particle counts were either low or showed no pattern with the solution pH. Visible particle scores were higher starting at pH 5.5–6.5. Although these scores are high, the samples were inspected near light, whereas higher particle counts are routinely observed. It was possible that the source material also contributed to the high particle levels, as it had reduced HCP levels due to further purification from protein A. This study indicated C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 100 that an optimum pH from a particle formation perspective would be pH 5 or pH . However, since it is understood that visible particle scores are overestimated in this case, the pH was not changed from pH 6.0 as a result of this study. c. Effect of the shipment The formulations needed to be robust for shipping, so they were tested at various protein and PS-20 concentrations in pre-filled syringes. The formulation with 2–100 g / L of anti-IL5R antibody and 0–0.05% PS-20 was tested under other constant conditions at 240 mM trehalose, 20 mM histidine / histidine HCl, and pH 6. Several other conditions at 2 g / L were tested, including glycine, calcium chloride, pH 5.5, pH 6.5, and 0.02% polysorbate-80. None of these conditions showed improvement over the trehalose formulation at pH 6 with polysorbate-20, so they are not discussed further. One milliliter of sample was loaded into a platform PFS containing 0.4 mg of silicone oil. The samples were shipped, stored at 5°C, 25°C, and 40°C, and tested over two months using visual inspection, MFI, and HIAC. The results are presented in Figure 7. The graph shows the subvisible particle counts from MFI after 1 month of storage at 25°C. C7QC Ln / I 7Π7 / Β / YILI 101 HIAC or after storage at other temperatures showed trends similar to the dataset shown. Visual inspections did not indicate high counts of visible particles for any of the samples except the one containing calcium chloride. The high protein concentration solutions (4–20 g / L) were robust against shipping as long as some PS20 was present. Therefore, the trehalose formulation was used in long-term stability studies for the 20–100 g / L solution. The shipping data confirmed that the low-concentration formulations were not robust, as evidenced by the high and highly variable subvisible particle counts. The data also showed that the problem was not resolved by using polysorbate alone; therefore, it was necessary to reformulate the low-concentration solutions. d. Reformulation of low concentration DS Low-concentration reformulation tests were stress-tested using simulated transport and tested using MFI. The subvisible particle counts shown were >10 pm particles, filtered aspect ratio; similar trends were observed for other particle sizes. During manufacturing, an unformulated drug substance (UDS) will be produced and frozen at high C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 102 concentration (k 100 g / L) containing trehalose. Storage of this high-concentration intermediate is necessary to allow dilution into various formulations across the 2100 mg / mL formulation range. Dilution of the UDS will result in some residual trehalose; for compositional uniformity, a single trehalose concentration will be used throughout the low-dose range. The AMP and pH were not changed. The first test was used to determine the minimum protein concentration at which the trehalose formulation was stable, and to determine the effect of increased ionic strength by formulating in 150 mM trehalose with 75 mM arginine HCl or sodium chloride. The results shown below indicate that protein concentrations > 10 g / L were stable, but for robustness, the low concentration range was set at 2–20 g / L. Increasing the ionic strength resulted in more stable solutions with both excipients. See, for example, Figure 8. The following studies focused on optimizing arginine or NaCl concentrations; a protein concentration of 2 g / L was used as the worst-case scenario for all studies. For each excipient, broad and narrow excipient concentration assays were performed using 0.02% PS-20. The initial arginine assay was performed with varying amounts of trehalose, where the following were prepared: 103 solutions were prepared combining 270 mM arginine with 250 mM trehalose. The aim was to maintain osmolality, but the calculation was performed incorrectly (arginine-HCl is bivalent), so the solutions containing arginine were hyperosmotic. The remaining excipient concentration tests were performed with a constant trehalose concentration of 40 or 50 mM, based on the residual trehalose at 20 g / L after dilution from the 100 g / L stock solution. The results are provided in Figures 9 and 10. Broad arginine and NaCl assays indicate that a higher concentration of arginine (50 mM) or NaCl (75 mM) is necessary to produce a stable formulation. Narrow concentration assays of arginine (75–150 mM) or NaCl (100–200 mM) resulted in low particle counts across the entire range. This suggests that a concentration in the middle of these ranges should produce a robust formulation; 130 mM was chosen to be isoosmotic in combination with 50 mM residual trehalose. The optimization of the PS-20 concentration for the new formulations was verified using the same method. These experiments were performed simultaneously with narrow excipient concentration tests, so a midpoint concentration was used. The conditions under which 104 tests were conducted with 0.01–0.1% PS-20, 115 mM arginine HCl, and 40 mM trehalose, and with 0.01–0.05% PS-20, 150 mM NaCl, and 50 mM trehalose. A couple of samples were tested with 0.02% PS-80, but the counts were higher than the corresponding PS-20 result (data not shown). Particle counts were low for all polysorbate levels tested, indicating that there is no need to change the level from 0.02% in new formulations. See, for example, Figure 11. The results of the reformulations for low concentrations of anti-IL5R antibody indicated that either arginine or NaCl could stabilize the formulation in the short term. The formulations considered were 130 mM arginine HCl or 130 mM NaCl, with 50 mM trehalose, 20 mM histidine / histidine HCl, 0.02% PS-20, pH 6 for protein concentrations of 2–20 g / L. e. Vial and PFS considerations The three formulations developed previously (20-100 mg / ml trehalose, 2-20 mg / ml trehalose / arginine, and 220 mg / ml trehalose / NaCl) were suitable for both vial and PFS configurations. The vial configuration was a 3 cc Schott vial with a West 4432 / 50 stopper. The greatest risk associated with the vial configuration was the level of silicone oil in the stoppers; therefore, long-term stability studies were conducted with 105 plugs that have a higher level of silicone oil (0.039 mg / cm2) than those that will be used generally (0.007 - 0.024 mg / cm2). The syringe tested with the anti-IL5R antibody formulation was the platform syringe, a BD 1 mi length PFS with a clipped tab, a stacked 29G thin wall needle, containing 0.4 mg of Si oil, and covered with a BD260 rigid needle sheath (catalog no. 47363119). f. Long-term stability studies Two long-term stability studies were conducted to verify the decisions made based on the screening studies. Stability study #1 investigated the long-term stability of trehalose and arginine / trehalose formulations in PFS and vials. Additionally, PFS comparisons were performed, which will not be discussed herein. Stability Study #2 was initiated to provide data from another batch of material for the configurations examined in Study #1, and also to investigate the NaCl / trehalose formulation grouping and the impact of fill volume from 1 ml to 1 ml in PFS and vials. i. Stability study no. 1: Stability of PFS presentations of anti-IL5R antibody Stability studies were performed on syringes with C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 106 vials were used as a control. Each formulation pool endpoint was tested in each primary container. The test syringe was the Biotech Hypak™ platform; this is a 1 ml long, virtually tungsten-free glass syringe from BD with a 29G thin-wall needle and 0.4 mg of silicone oil. The vials used were 3 cc Schott vials with West 4423 / 50 stoppers and counterseals. The loaded formulations are as follows: • 2 and 20 mg / ml of anti-IL5R antibody, arginine HCI 125 mM, trehalose 50 mM, histidine / histidine HCI 20 mM, 0.02% PS-20, pH 6; and • 20 and 100 mg / ml of anti-IL5R antibody, trehalose 250 mM, histidine / histidine HCI 20 mM, 0.02% PS-20, pH 6. A. Purity of pre-filled syringe presentations with anti-IL5R antibody There was no significant effect of the primary container on monomer loss for any formulation. Some impact of protein concentration was observed, but the monomer loss rate was consistently low. See Figure 12A. B. Particle analysis of pre-filled syringe presentations with anti-IL5R antibody Particle formation was thought to be the main degradation pathway of anti-IL5R antibodies. C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 107, a method thought to play a major role in determining the appropriate PFS. Measurement of subvisible particles using HIAC showed an increase in the number of particles at the PFS, likely due to silicone oil droplets (see Figures 12B and 12C). However, total particle counts remained well below the USP limits of 6,000 particles >10 pm / mi and 600 particles >25 pm / mi for all configurations. MFI was used as an orthogonal method and showed similar results, although less difference was observed between vessels since silicone oil droplets can be removed by filtering the results in the MFI software. ii. Summary of stability in Hypak™ for Blotech syringes at 5°C Table 1 shows a summary of the stability data (Stability Study No. 1) available for anti-IL5R antibody in Biotech Hypak™ syringes at 5°C for up to 16 months for arginine formulations and 24 months for trehalose formulations. Visually detected particles led to a reduction in PS-20 concentration from 0.02% to 0.006%. No other high risks were identified, although subvisible particle counts were C7QC Ln / I 7Π7 / Β / ΥΙΛΙ variables. 108 TABLE 1 C70C Ln / ί7Π7 / E / YΙΛΙ Result range for all tested time points Assay 2 mg / ml Arg 20 mg / ml Arg 20 mg / ml Tre 100 mg / ml Tre Appearance (visible particles, worst observation) < SD 1 = SD 4 = SD 2 < SD 3 HIAC (particles / ml) > 10 pm < 590 < 3,000 < 1,800 < 2,000 > 25 pm < 30 < 20 < 30 < 60 MFI (particles / ml) > 10 pm < 110 < 2,200 < 1,400 < 1,700 > 25 pm < 50 < 100 < 60 < 480* SEC (% mon. loss / year) 0% 0.1% 0.1% 0.2% RP (% fragment) < 2.0% < 1.8% < 1.9% < 1.9% Functional forces using Instron (initial and sliding force) < 6N < 7N < 7N < 12N Bioassay (% of power) 93 116% 92 - 103% 95 111% 88 - 99% Reduced Bichannel Conforms to reference pattern. Not reduced Conforms to reference pattern. cIEF Conforms to reference pattern. Summary of anti-IL5R antibody stability in multiple formulations in Biotech Hypak syringes at 5°C for 16 months. Appearance results included particulate matter, which was mitigated by reducing the concentration of 109 PS-20 (covered in a separate report). Subvisible particle results were variable, but no trends were observed. All other results are within expectations for a stable product. * iii. Stability Study No. 2 Stability Study No. 2 was a pooled stability study in pre-filled syringes and vials, designed to decide the low-dose formulation and fill volume, and to verify placebo stability. The previous stability study used to select the PFS had a fill volume of only 1 ml. However, there were several potential benefits to a lower fill volume, including reduced pain at injection, a smaller lump under the skin, faster administration, and less leakage from the injection site. The pooling strategy for the 1 mL fill option consisted of two protein concentration pools: 2–20 g / L for the low dose and 20–100 g / L for the high dose. The same pooling for a h mL fill covered the 1–50 mg dose range and also required a fill volume pool of 100 g / L from -1 mL for the 50–100 mg dose. This is shown graphically in Figure 13 for clarity. In both cases, the lowest dose pool was studied in formulations. C70C Ln / ί7Π7 / E / YΙΛΙ 110 based on both arginine and NaCl. The pharmacological substances and loaded placebos were as follows: • All solutions: 20 mM Histidine / Histidine HCl, 0.02% PS-20, pH 6.0 • 2 Arg / 20 Arg: 2 or 20 g / 1 anti-IL5R antibody, 125 mM arginine HCl, 50 mM trehalose • 2 NaCl / 20 NaCl: 2 or 20 g / 1 anti-IL5R antibody, NaCl 130 mM, 50 mM trehalose • 20 Tre / 100 Tre: 20 or 100 g / 1 anti-IL5R antibody, 250 mM trehalose • Arg placebo: 125 mM Arginine HCl, 50 mM trehalose • NaCl placebo: 130 mM NaCl, 50 mM trehalose • Tre placebo: 250 mM Trehalose The 1 ml fill volume was not tested for any of the vial configurations or the placebo in PFS in order to reduce the overall study size, since the 1 / 2 ml fill volume was the most likely worst-case configuration due to the higher surface area to volume ratio. All samples were sent and then stabilized at 5, 25, and 40°C. The vials were stored inverted during stabilization to maximize contact with the stopper. By the time the visible particles were discovered in earlier studies, they had C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 111 collected 6 weeks of data for this stability study. Additionally, particulate matter was observed in the NaCl formulation between the 3 and 6 month time points of this study (data not shown), which led to the rejection of the NaCl formulation in favor of the arginine formulation. The additional formulation work required to mitigate visible particle formation is described in the following examples and resulted in a decrease in the polysorbate-20 concentration from 0.02% to 0.006%. No other stability issues were observed for this formulation, and no significant impact of container or fill volume was observed. One year of stability data is summarized in Figure 14, including visible particle scores, loss of purity by SEC, particle counts by HIAC, and potency (not all configurations were tested at all time points). Conclusion of example 1 The formulation was tested using various stress methods, including freeze / thaw, agitation, known silicone oil additions, and accelerated stability testing. Long-term stability was used to verify the test results. The phase trehalose formulation C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 112 2b was satisfactory for high-concentration liquids with an increased polysorbate concentration, but showed instability when extended to low-concentration liquids, mainly through the formation of subvisible particles. The low-concentration range was reformulated by increasing the ionic strength with either arginine hydrochloride or sodium chloride, resulting in a stable solution. In order to cover the wide range of possible doses (2 - 100 mg), the three possible formulation groupings were as follows: • 2-20 g / 1, arginine hydrochloride 130 mM, trehalose dihydrate 50 mM, histidine / histidine hydrochloride 20 mM, 0.02% polysorbate-20, pH 6.0; • 2-20 g / 1, sodium chloride 130 mM, trehalose dihydrate 50 mM, histidine / histidine hydrochloride 20 mM, 0.02% polysorbate-20, pH 6.0; and • 20-100 g / 1, trehalose dihydrate 250 mM, histidine / histidine hydrochloride 20 mM, 0.02% polysorbate-20, pH 6.0. The long-term stability study of up to 24 months indicates that all three formulations were stable at 2–8°C with respect to agitation, relatively insensitive to silicone oil, and compatible with vials and PFS. Additionally, minimal degradation was observed at C70C Ln / ί7Π7 / E / YΙΛΙ 113 elevated temperatures. Continuous observations of the two low-concentration formulations eliminated the NaCl option due to increased visible particle formation compared to the arginine option, resulting in two formulation groupings. The data indicated that pre-filled syringes are an acceptable primary container with a fill volume of either 1 ml or 7 ml. Visible particle formation remained an issue with these formulations, as discussed in the following examples. Example 2 - Particle formation in anti-IL5R antibody formulations Visible particles were detected in aqueous anti-IL5R antibody formulations in both vials and PFS in previous long-term stability studies, with the first detection occurring at the 6-month time point (data not shown). A study was conducted to mitigate the formation of visible particles in an anti-IL5R antibody formulation comprising polysorbate 20 (PS-20) stored for an extended period. The following example describes a long-term study of formulations comprising various concentrations of PS-20 and protein to verify the significance of PS-20 concentration in mitigating particle formation. This study resulted in a range C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 114 acceptable from 0.002 - 0.01% of PS-20. C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ Abbreviations and definitions Abbreviation Definition Abbreviation Definition cIEF Capillary Isoelectric Focusing MFI Microflow Imaging DLS Dynamic Light Scattering PS Polysorbate DP Drug Product PFS Prefilled Syringe DS Drug Substance RP Reversed-phase chromatography FC Flow cytometry SEC Size exclusion chromatography Abbreviation Definition Arg Arginine formulation: Arginine HCl 130 mM, trehalose dihydrate 50 mM, histidine / histidine HCl 20 mM, pH 6.0, various PS-20 Tre Trehalose formulation: Trehalose dihydrate 250 mM, histidine / histidine HCl 20 mM, pH 6.0, various PS-20 Preliminary studies Particle formation was detected in the long-term stability studies described in Example 1. However, the particles were extremely small and resembled a cloud more than individual particles. 115 In order to observe the particles, the samples were inspected near the light source. Since the particles were different from those in the standard sets in the vial and PFS, the samples were compared to each other as standards at each time point. Particles were first detected at the 6-month time point in 100 g / 1 vials of Tre containing 0.02% PS-20. Six-month and 11-month samples were compared in (1) vials and (2) pre-filled syringes (PFS). Both studies showed that particle formation was more intense in vials than in PFS, although PFS standards were not available at the time, so a numerical comparison is not possible. Samples were decanted from the PFS and injected into vials for appearance testing. No more particles were observed in these vials, verifying that the difference is not a path length effect. In trehalose formulations, this difference between vial and PFS is more significant than in arginine formulations. A comparison was made of the various PS-20 concentrations (0, 0.01, 0.02, and 0.03%) in 100 g / L Tre formulations, both in vials and as post-shipment PFS. The lower PS-20 concentrations of 0 and 0.01% were completely free of particles. 116 at the 11-month time point. Particles were visible in both the vial and the PFS at 0.02% and 0.03% PS20. At 20 months, the PFS with 0% and 0.01% PS-20 and the vial with 0% PS-20 remained clear, but the vial with 0.01% PS-20 had a very small tornado of particles. In targeted studies, when held near a light source, particles were clearly visible in 100 g / L Tre PFS vials containing 0.02% PS-20, in some cases as early as 3–4 months. At the low concentration end (20 g / L) of the Tre pool, particles formed much more slowly and were observed only in vials at 21 months. No particles have been observed in PFS containing 20 g / L Tre at any PS-20 concentration, with data available up to 21 months. Particle formation in arginine formulations was somewhat slower, with particles observed at the high concentration end (20 g / L) of the pool containing 0.02% PS-20 at 6–9 months. Particles have never been observed in the 2 g / L Arg formulation at any PS-20 concentration in any container, with data available up to 16 months. Stress and accelerated temperature studies provided no data on particle formation. At 40 °C, no particles formed at all during the 3-month testing period. At 25 °C, particle formation 117 particles was similar or slightly reduced compared to 5 °C. These data indicated that the high protein concentration extremes of the pool were at high risk of visible particle formation, while the low concentration extremes were potentially at long-term risk. Reducing the PS-20 concentration to mitigate particle formation was investigated. The primary vessel remained the platform PFS, and vials were used as an early readout of particle formation since particle formation in vials was more intense and easier to observe. Investigation of various concentrations of PS-20 An extensive stability study was designed to investigate particle formation in various formulations, PS-20 concentrations, and antibody concentrations. All samples were loaded into both PFS and vials, shipped twice to a separate location to simulate the distribution process, and placed in stability conditions at 5 °C. Appearance testing was performed monthly. SEC, HIAC, and MFI tests were also performed on a subset of samples at time zero, 3, 6, and 9 months. Figure 15 shows the samples that were prepared as part of this study. Without any PS-20, subvisible particles formed 118 after shipment, as shown by the MFI data in Figure 16 for PFS at time zero. The lowest tested level of PS-20 (0.002%) or higher was sufficient to protect against shipping stress. Additionally, the lowest PS-20 concentration (0.002%) was verified to be sufficient to protect against DS shipping stress in a tank using a reduced-scale model (data not shown herein). The particle appearance results showed significant particle formation in vials above 0.01% PS-20, and some particle formation in PFS at 0.02% PS-20 for both formulation groups, with fewer particles observed at the lower concentration end of both groups. See Figures 17A-17D. The first particle observations were at 3 months for 100 g / L of Tre and at 6 months for 20 g / L of Arg. The figures illustrate the impact of protein and PS-20 concentration on particle formation at the final time point, 9 months. Note that all particle formation observations were made close to the light source. Appearance data establishes an upper limit on PS-20 concentration of 0.01% and subvisible particle counts establish a lower limit of 0.002% (based on available data, the actual limit C70C Ln / ί7Π7 / E / YΙΛΙ 119 may be lower). The midpoint of this acceptable interval (0.006%) was established as the new PS-20 concentration. Global stability for PFS was verified for end-group samples, including up to 9 months of data for 2 g / L Arg and 20 g / L Arg, and up to 18 months of data for 20 g / L Tre and 100 g / L Tre. The following assays were tested: A. 0.002, 0.006 and 0.01% of PS-20: Appearance, HIAC, MFI and SEC. B. 0.006% PS-20 only: Instron, BioAssay, BioAnalyzer, RP and cIEF. All data indicate that the formulation was stable and low-risk. A summary of the data is shown in Table 2. C70C Ln / L7n7 / B / YIAI TABLE 2 Assay Results for all samples tested Appearance (visible particles, worst observation) < 2 OD HIAC (particles / mi) > 10 pm < 640 / mi > 25 pm < 30 / mi MFI (particles / mi) > 10 pm < 610 / mi > 25 pm < 60 / mi SEC (% monomer loss / year) 0.0 - 0.4% / year RP (% fragment) < 1.8% Initial Strength < 8.5 N 120 Functionality using Instron Sliding force < 11.8 N Bioassay (% of power) 86 - 109% Bioanalyzer Reduced Agrees ref. with pat. of Not reduced Agrees ref. with pat. of cIEF Agrees ref. with pat. of C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ The available data from example 2 indicated that reducing the concentration of PS-20 to 0.006% mitigated particle formation and produced an antibody formulation product that was stable for at least 9 months (arginine formulation) or 18 months (trehalose formulation), with no indication of imminent failure. Example 3 Orthogonal methods for particle detection The primary method for particle detection and quantification was appearance testing by visual inspection, as exemplified in Example 2. Visual inspection was variable for several reasons. In general, visual inspection varied due to the inherent variability of human perception, leading to different results for different individuals. Due to the very small size of these particles, their visibility was highly dependent on the amount of light and differed from the particle patterns for both vials and PFS. These factors 121 increased the variability of results between time points and between analysts. Orthogonal methods were investigated to verify the appearance results. The particles formed in the trehalose formulations were too small to be seen individually, so subvisible particle methods were investigated. The worst-case sample (100 g / L of Tre, 0.02% PS-20, vial) from various batches was compared at 2 weeks, and 2, 5, and 9 months using DLS, FC, HIAC, and MFI. The DLS was performed at 100 g / L, leading to an underestimation of the main peak, as expected, and a lack of reliability in all peak sizes. Large peaks were detected for the 2, 5, and 9-month samples, with a size of 1.4–2.2 µm. Although the reported size was unreliable, the presence of the peaks correlated with visible particles. However, neither the reported particle size nor the intensity of the particle peak correlated with the visual appearance results. The HIAC results were similar for all samples; no particles were detected. MFI counts for particles >10 µm and >25 µm were similar across all samples. However, MFI counts for particles >1 µm and >2 µm, as well as FC counts, showed a trend consistent with the visual appearance results. 122 and increase with the age of the sample. The results of these samples are shown in Figure 18. Additional experiments indicate that >lpm particles using MFI provide more reliable trends with visual appearance results than larger particles or FC counts (data not shown). Similar experiments were performed with 20 g / L samples of Arg showing visible particles, but none of the orthogonal methods were satisfactory for detecting these particles. The particles formed in arginine formulations appeared much larger than those formed in trehalose and were observed as individual particles, which was likely because they were not detected by subvisible particle methods. MFI was used to verify the effect of PS-20 concentration in Example 2. The comparison of MFI and appearance scores is shown in Figures 19A and 19B for Example 2 at the 9-month time point. Along with additional measurements (not shown), the comparison indicated that particles were visible when the MFI count exceeded approximately 100,000 particles >lpm / mi. The MFI results provided further support for the conclusion that particle formation was mitigated by 0.002–0.01% PS-20, particularly in PFS. Vial data were considered the worst-case scenario and were also C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 123 stable at the target concentration of 0.006% PS-20. Example 4 Stability study An additional stability study was conducted to investigate all configurations from previous studies with the new target PS-20 concentration of 0.006%, and to further enhance the stability of these formulations. The grouping included a protein concentration group as well as a fill volume group and is shown graphically in Figure 20. The addition of the fill volume grouping increased the dosage range covered by the trehalose formulation. These additional configurations reduced the risk associated with the arginine formulation, which had a higher risk because the particles form more slowly and cannot be detected by orthogonal methods. The samples included in this stability study were: • 0, 2 and 20 g / 1, 1 ml fill, arginine formulation, 0.006% PS-20; • 0 and 2 g / 1, 0.3 ml fill, arginine formulation, 0.006% PS-20; • 0, 20, 50 and 100 g / 1, 1 ml fill, trehalose formulation, 0.006% PS-20; and • 0 and 20 g / 1, 0.3 ml fill, trehalose formulation, 0.006% PS-20. C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 124 The samples were sent to an external location twice to simulate the distribution process and then placed in stability at 5°C, 25°C and 40°C. Nine months' data were collected for the arginine formulations, and twelve months' data were collected for the trehalose formulations. The results were consistent with historical data, and no particulate matter was observed in these samples up to this point. Furthermore, no trends in subvisible particulate matter were observed over time, although a few moderately high outliers were found. The range of results for all assays is shown in Table 3. TABLE 3 C70C Ln / ί7Π7 / E / YΙΛΙ Result range for all tested samples Assay 5°C (9-month Arg or 12-month Tre formulations) 25°C (6 months) 40°C (1 month) Appearance (visible particles, worst observation) = SD 0 < SD 1 = SD 0 HIAC (particles / mi) > 10 µm < 2,400 / mi < 1,900 / mi < 1,900 / mi > 25 µm < 110 / mi < 1101 / mi < 100 / mi 125 MFI (particles / mi) > 10 µm < 100 / mi < 700 / mi < 50 / mi > 25 µm < 50 / mi < 40 / mi < 10 / mi SEC (monomer loss) 0 - 0.3% / year 0.1 - 0.6% / month 2.2 - 3.5% / month RP (% of fragment) < 1.7% < 3.6% < 4.4% Functional forces by Instron (initial and sliding force) < 11.7 N Not evaluated Not evaluated Bioassay (% of power) 84 - 122% 83 - 113% 83 - 110% Bioanalyzer Reduced Agrees with reference pathogen Not reduced Agrees with reference pathogen cIEF Agrees with reference pathogen Does not agree with reference pathogen at 1 month C70C Ln / ί7Π7 / E / YΙΛΙψ43 of 44 measurements were in this range, but an atypical result of 347 particles / ml was also measured. The data supported the recommendation of this formulation grouping for the entire dosage range. The trehalose grouping had less risk than the arginine grouping and was recommended for doses as low as 6 mg. Conclusion of examples 2-4 Particle observations in previous long-term stability studies led to an investigation 126 formulation variables that could be altered to improve stability were analyzed and tested. The key variables, protein and polysorbate concentrations, were analyzed and tested. Based on the data presented above, a permissible polysorbate range of 0.002% to 0.01% and a target of 0.006% were determined to be optimal formulations for the anti-IL5R antibody formulation. This observation was supported by two stability studies with 18 and 12 months of available data, primarily through visual appearance tests. It was also observed that the trehalose formulation could be used instead of the arginine formulation in the 6–20 mg range using a volume pool of 0.31.0 mL at 20 mg / mL. The trehalose formulation was found to be more predictable than the arginine formulation due to the larger dataset and better detection. Example 5 Further purification was undertaken, focusing on the reduction of the host cell protein (HCP), to determine the effect of HCP on particle formation. Anti-IL5R antibody was purified as briefly described in Figure 21. Two-dimensional gel analysis of the unretained fraction of the protein A column indicated that they were C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ 127 Several protein species were present. See, for example, Figure 22. The major impurities, as determined by reversed-phase mass spectrometry (RP-MS), included approximately 60% Fab fragment, approximately 5% light chain (LC) and fragments, and approximately 40% host cell proteins (HCPs) unrelated to anti-IL5R antibody. The HCPs unrelated to anti-IL5R antibody included glutathione Stransferase (GST), fructose-bisphosphate aldolase, and transaldolase. The unretained fraction from the protein A column was further passed through a protein L column to further separate (1) the Fab fragments from (2) the HCPs unrelated to anti-IL5R antibody. Some material in the HCPs unrelated to anti-IL5R antibody was found to be responsible for particle formation, and not the Fab fragments (data not shown). To determine that the major HCPs were responsible for particle formation, GST was investigated first. The role of GST in particle formation was investigated by (1) selective removal of GST to determine the effect on particle formation, (2) particle sediment analysis to determine the presence of GST in the sediment, and (3) addition of GST to anti-IL5R antibody formulations to 128 determine the effect on particle formation. Preliminary evidence of specific GST removal using an affinity matrix from a glutathione-sepharose conjugate suggested that GST removal resulted in reduced particle formation (data not shown). Analysis of sediments formed from the non-retained fraction of protein A indicated high GST concentrations in the sediments (data not shown). GST (i.e., known additions) was added to purified, particle-free anti-IL5R antibody formulations to determine the effect of GST on particle formulations. GST was obtained from a commercial source (Prospec). GST was added to a formulation comprising 50 mg / mL anti-IL5R antibody, 20 mM histidine HCl buffer, 9% (w / v) trehalose, 0.02% PS-20, pH 6.0, resulting in GST concentrations of 3.8 pg / mg and 7.6 pg / mg. Samples were incubated at 38–42°C. Particle formation was observed by placing the samples in a light box. The incubation time required to observe particle formation depended on the level of GST present. For GST samples with known additions of both 3.8 pg / mg and 7.6 pg / mg, particles were observed after 24 hours at 38-42°C (data not shown). These results suggested that the known additions C7QC Ln / Lznz / E / YILI 129 of GST to anti-IL5R antibody formulations causes particle formation in the anti-IL5R antibody formulation. Example 6 The activity of GST was investigated in various anti-IL5R antibody formulations purified by different methods. As a preliminary step, a GST activity assay (BioVision) was used to determine GST concentrations and establish a standard curve. GST catalyzes the formation of the thiol group of glutathione (GSH) with electrophilic compounds such as 1-chloro-2,4-dinitrobenzene (CDNB) to form a GS-DNB conjugate that is detectable at 340 nM. Therefore, the increase in absorbance at 340 nM is directly proportional to GST activity. Using this assay, the GST concentration was determined for various anti-IL5R antibody formulations (AJ samples) purified by different procedures. The correlation between GST concentration and particle formation was observed. The results are presented in Table 4. Table 4 C70C Ln / ί7Π7 / E / YΙΛΙ Sample GST Concentration Particle Description A 188.4 High number of particles (maximum) B 0.422 Virtually free* 130 c 2.074 Practically free* D 1930.5 High number of E particles 1950.6 High number of F particles 1774.2 High number of G particles 40.6 Formation of H particles 1.073 Some particles I CLLOQ Particle-free J 5.416 Formation of particles * Some, but not many, particles. LLOQ = lower limit of quantification. This evidence confirms that the presence of GST is correlated with particle formation. Example 7 Various purification columns were investigated to identify the most effective method for reducing the GST concentration in an anti-IL5R antibody formulation. See Table 5. The GST concentration was determined as briefly explained in Example 7. 131 C7QC Ln / ίZΖΠΖ / Β / YΙΛΙ Table 5 Description GST Concentration (pg / ml) CM Product 5.935 HA Product 1.255 MabSelect Sure Elut Product <lloq producto de captoadhere <lloq cex* 9.228 21.081* The GST concentrations of two separate batches of anti-IL5R antibodies were determined. Table 5 suggests that both the protein A column (MabSelect Sure) and the mixed-mode chromatography column (CaptoAdhere) were satisfactory in reducing the GST concentration below a detectable level during purification of the anti-IL5R antibody. Example 8 The presence of GST was investigated in other antibody preparations. The presence of particles in these antibody preparations was also investigated. The results are presented in Table 6, with commentary. Table 6 C70C Ln / ί7Π7 / E / YΙΛΙ Antibody formulation: Was active GST detected? Was there a trend with particle formation? Comments Anti-IL5R Yes Yes N / A Yes N / A Insufficient particle data to determine a trend B No (except 1 sample) No Suggests that GST may not be the cause of particle formation for this antibody. C Yes N / A Active GST, but no particle formation D Yes N / A Insufficient particle data to determine a trend All the different embodiments or options described herein can be combined in any and all of their variations. Although the invention has been presented and described particularly with reference to some embodiments thereof, those skilled in the art will understand that these have been presented only for illustrative purposes and without limitation, and that various changes can be made to the 133 form and details of the present without departing from the nature and scope of the invention. Therefore, the extent and scope of the present invention shall not be limited by any of the illustrative embodiments described above, but shall be defined solely in accordance with the following claims and their equivalents. All documents cited herein, including journal articles or abstracts, corresponding or published foreign or U.S. patent applications, foreign or filed patents, or any additional documents, are each incorporated herein in full by reference, including all data, tables, figures, and text contained in the cited documents. It is hereby stated that, as of this date, the best method known to the applicant for putting the aforementioned invention into practice is the one that is clear from the present description of the invention.< / lloq>

Claims

1. A stable, aqueous antibody formulation, characterized in that it comprises: a. from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and b. from approximately 0.002% to approximately 0.01% of polysorbate-20.

2. Antibody formulation according to claim 1, characterized in that it further comprises an uncharged excipient.

3. Antibody formulation according to claim 2, characterized in that the uncharged excipient is trehalose.

4. Antibody formulation according to any of claims 1 to 3, characterized in that it comprises approximately 2 to approximately 20 mg / ml of the antibody.

5. Antibody formulation according to any of claims 1 to 3, characterized in that it comprises from approximately 20 to approximately 100 mg / ml of the antibody.

6. Antibody formulation according to claim 4, characterized in that the concentration of unloaded excipient is from approximately 20 mM to approximately 80 mM.

7. Antibody formulation according to claim 5, characterized in that the concentration of unloaded excipient is approximately 200 mM to approximately 400 mM.

8. Antibody formulation according to claim 4, characterized in that it further comprises arginine.

9. Antibody formulation according to claim 8, characterized in that the arginine is LArginine.

10. Antibody formulation according to claim 8, characterized in that it comprises approximately 100 mM to approximately 200 mM of L-Arginine.

11. Antibody formulation according to C70C Ln / 17P7 / E / YILI 136 claim 8, characterized in that it comprises approximately 120 mM to approximately 140 mM of L-Arginine, and approximately 40 mM to approximately 60 mM of uncharged excipient.

12. Antibody formulation according to any of claims 1 to 11, characterized in that it further comprises histidine.

13. Antibody formulation according to claim 12, characterized in that the histidine concentration is from approximately 15 mM to approximately 30 mM.

14. Antibody formulation according to any of claims 1 to 13, characterized in that the antibody is not subjected to lyophilization.

15. Stable, aqueous antibody formulation, characterized in that it comprises from approximately 2 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the formulation is stable after storage at approximately 40°C for at least 1 month.

16. A stable, aqueous antibody formulation characterized in that it comprises: a. from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, b. from approximately 0.002% to approximately 0.01% of polysorbate-20, c. from approximately 40 mM to approximately 60 mM of trehalose, d. from approximately 110 mM to approximately 150 mM of L-arginine, and e. from approximately 15 to approximately 30 mM of histidine.

17. A stable, aqueous antibody formulation characterized in that it comprises: a. from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, b. from approximately 0.002% to approximately 0.01% of polysorbate-20, c. from approximately 200 mM to approximately 300 mM of trehalose, and d. of approximately 15 to approximately 30 mM of histidine.

18. Stable, aqueous antibody formulation characterized in that it comprises: a. from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, b. approximately 0.006% of polysorbate-20, c. approximately 50 mM of trehalose, d. approximately 130 mM of L-arginine, and e. approximately 20 mM of histidine.

19. A stable, aqueous antibody formulation characterized in that it comprises: a. from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, b. approximately 0.006% polysorbate-20, c. approximately 250 mM trehalose, and d. approximately 20 mM histidine.

20. A stable, aqueous antibody formulation, characterized in that it comprises: a. approximately 30 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 of C7QC Ln / ίZЖРZ� / B / YILI 140 according to the Kabat numbering system of SEQ ID NO: 8-10, b. approximately 0.006% of polysorbate-20, c. approximately 250 mM of trehalose, and d. approximately 20 mM of histidine.

21. Antibody formulation according to any of claims 1 to 20, characterized in that the formulation is stable after storage at approximately 25°C for at least 3 months.

22. Antibody formulation according to any of claims 1 to 21, characterized in that the formulation is stable after storage at approximately 5°C for at least 18 months.

23. Antibody formulation according to any of claims 1 to 22, characterized in that the antibody stored at approximately 40°C for at least 1 month retains at least 80% of the IL-5R polypeptide binding capacity compared to a reference antibody that has not been stored.

24. An antibody formulation according to any one of claims 1 to 23, characterized in that the antibody stored at approximately 5°C for at least 6 months retains at least 80% of the binding capacity to an IL-5R polypeptide compared to a reference antibody that has not been stored. C7QC Ln / įZРZ� / B / YILI 141 25. Antibody formulation according to any of claims 1 to 24, characterized in that the antibody stored at approximately 40°C for at least 1 month retains at least 95% of the binding capacity to an IL-5R polypeptide compared to a reference antibody that has not been stored.

26. Antibody formulation according to any of claims 1 to 25, characterized in that the antibody stored at approximately 5°C for at least 6 months retains at least 95% of the IL-5R polypeptide binding capacity compared to a reference antibody that has not been stored.

27. Antibody formulation according to any of claims 1 to 26, characterized in that less than 2% of the antibody forms an aggregate after storage at approximately 40°C for at least 1 month as determined by HPSEC.

28. Antibody formulation according to any of claims 1 to 27, characterized in that less than 2% of the antibody forms an aggregate after storage at approximately 5°C for at least 12 months as determined by HPSEC.

29. Antibody formulation according to any of claims 1 to 28, characterized in that the formulation is substantially free of C7QC Lh / įZЖРZ� / B / YILI 142 particles after storage at approximately 40°C for at least 1 month as determined by visual inspection.

30. Antibody formulation according to any of claims 1 to 29, characterized in that the formulation is substantially free of particles after storage at approximately 5°C for at least 12 months as determined by visual inspection.

31. Antibody formulation according to any of claims 1 to 30, characterized in that the formulation is an injectable formulation.

32. Antibody formulation according to any of claims 1 to 31, characterized in that the formulation is suitable for intravenous, subcutaneous or intramuscular administration.

33. Sealed container characterized in that it contains the antibody formulation in accordance with any of claims 1 to 32.

34. Unit-dose pharmaceutical form suitable for parenteral administration to a human being, characterized in that it comprises the formulation of antibodies in accordance with any of claims 1 to 32 in a suitable container.

35. Unit-dose pharmaceutical form of C7QC Ln / įZРZ� / B / YILI 143 in accordance with claim 34, characterized in that the antibody formulation is administered intravenously, subcutaneously or intramuscularly.

36. Unit-dose pharmaceutical form according to claim 34 or 35, characterized in that the suitable container is a pre-filled syringe.

37. Unit-dose pharmaceutical form according to claim 36, characterized in that the pre-filled syringe comprises a needle.

38. Unit dosage pharmaceutical form according to claim 37, characterized in that the needle is a 29G thin-walled needle.

39. Unit dosage pharmaceutical form according to any of claims 36 to 38, characterized in that the pre-filled syringe is a plastic syringe or a glass syringe.

40. Unit-dose pharmaceutical form according to any of claims 36 to 39, characterized in that the pre-filled syringe is made of materials that are substantially tungsten-free.

41. A unit-dose pharmaceutical form according to any of claims 36 to 40, characterized in that the pre-filled syringe is coated with silicone. C70C Ln / ί7Π7 / E / YΙΛΙ 42. Unit-dose pharmaceutical form of 144 in accordance with any of claims 36 to 41, characterized in that the pre-filled syringe comprises a plunger having a fluoropolymer resin disc.

43. A pre-filled syringe characterized in that it comprises: a. from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and b. from approximately 0.002% to approximately 0.01% of polysorbate-20.

44. Pre-filled syringe according to claim 38, characterized in that it further comprises: c. from approximately 40 mM to approximately 60 mM of trehalose, and d. from approximately 110 mM to approximately 150 mM of L-arginine.

45. Pre-filled syringe characterized in that it comprises: a. from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises an amino acid sequence of SEQ ID NO:1, C70C Ln / ί7P7 / E / YILI 145 b. from approximately 0.002% to approximately 0.01% of polysorbate-20.

46. ​​Pre-filled syringe according to claim 40, characterized in that it further comprises: c. approximately 200 mM to approximately 300 mM of trehalose.

47. A pre-filled syringe characterized in that it comprises: a. from approximately 2 mg / ml to approximately 20 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and b. approximately 0.006% polysorbate-20.

48. Pre-filled syringe according to claim 47, characterized in that it further comprises: c. approximately 50 mM of trehalose, and d. approximately 130 mM of L-arginine.

49. A pre-filled syringe characterized in that it comprises: a. from approximately 20 mg / ml to approximately 100 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, b. approximately 0.006% of polysorbate-20.

50. Pre-filled syringe according to claim 49, characterized in that it further comprises: c. approximately 250 mM of trehalose.

51. Pre-filled syringe characterized in that it comprises: a. approximately 30 mg / ml of an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, and b. approximately 0.006% polysorbate-20.

52. Pre-filled syringe according to claim 51, characterized in that it further comprises c. approximately 250 mM of trehalose.

53. Kit characterized in that it comprises the formulation C70C Ln / ί7Π7 / E / YΙΛΙ 147 according to any of claims 1 to 32, the container according to claim 33, the unit dosage form according to any of claims 34 to 42 or the pre-filled syringe according to any of claims 43 to 52.

54. A method for producing a stable, aqueous antibody formulation, characterized in that it comprises: a. purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy-chain variable region and a light-chain variable region, wherein the heavy-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light-chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; b. placing the isolated antibody into a stabilizing formulation to form the stable, aqueous antibody formulation, wherein the resulting stable, aqueous antibody formulation comprises: i. from approximately 2 mg / ml to approximately 100 mg / ml of the antibody, and ii. from approximately 0.002% to approximately 0.01% of polysorbate-20.

55. Method for preparing a stable, aqueous antibody formulation, characterized in that it comprises: a. purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; b. diluting the antibody from approximately 2 mg / ml to approximately 20 mg / ml in a solution comprising: i. from approximately 0.002% to approximately 0.01% of polysorbate-20, ii. from approximately 40 mM to approximately 60 mM of trehalose, and iii. from approximately 110 mM to approximately 150 mM of L-arginine.

56. A method for preparing a stable, aqueous antibody formulation, characterized in that it comprises: a. purifying an antibody from approximately 1 mg / ml to approximately 400 mg / ml, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10; b. diluting the antibody from approximately 20 mg / ml to approximately 100 mg / ml in a solution comprising: i. approximately 0.002% to approximately 0.01% polysorbate-20, and ii. of approximately 200 mM to approximately 300 mM of trehalose.

57. A method for producing a reconstituted antibody formulation comprising an antibody in which the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, characterized in that it comprises: a. purifying the antibody from a cell culture; b. lyophilizing the isolated antibody; c. adding the lyophilized antibody to an aqueous solution to form a reconstituted antibody formulation, wherein the reconstituted antibody formulation comprises: i. from approximately 2 mg / ml to approximately 100 mg / ml of the antibody, and ii. from approximately 0.002% to approximately 0.0.1% polysorbate-20.

58. An antibody formulation characterized in that it comprises an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, wherein the antibody formulation is essentially particle-free.

59. Antibody formulation, characterized in that it comprises an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2 and CDR3 according to the Kabat numbering system C70C Ln / ί7P7 / E / YILI 151 of SEQ ID NO: 8-10, wherein the antibody formulation is essentially free of active glutathione Stransferase (GST).

60. Antibody formulation according to claim 59, characterized in that the antibody sequence is essentially GST-free.

61. Antibody formulation according to claim 58, characterized in that it is essentially free of particles for at least 1 month when stored at 38-42°C.

62. Antibody formulation according to claim 58, characterized in that it is essentially particle-free for at least 6 months when stored at 2-6°C.

63. A method for purifying an antibody, wherein the antibody comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 5-7, and wherein the light chain variable region comprises the sequences CDR1, CDR2, and CDR3 according to the Kabat numbering system of SEQ ID NO: 8-10, characterized in that it comprises: a. obtaining a cell culture comprising the antibody, C7QC Ln / ίZЖРZ / B / YILI 152 b. performing affinity chromatography on the antibody, c. performing cation exchange on the antibody, d. performing mixed-mode chromatography on the antibody.

64. Method according to claim 63, characterized in that it further comprises a virus deactivation process.

65. Method according to claim 63, characterized in that it further comprises a diafiltration process.

66. A method for treating a pulmonary disease or disorder in a subject, characterized in that it comprises administering a therapeutically effective amount of the antibody formulation according to any of claims 1 to 32, the container according to claim 33, the unit dosage form according to any of claims 34 to 42, or the pre-filled syringe according to any of claims 43 to 52.

67. Method according to claim 49, characterized in that the pulmonary disease or disorder is an eosinophilic disease or disorder.

68. Method according to claim 49, characterized in that the pulmonary disease or disorder is C7QC Ln / įZРZ / B / YILI 153 asthma, COPD, eosinophilic asthma, combined eosinophilic and neutrophilic asthma, aspirin-responsive asthma, allergic bronchopulmonary aspergillosis, acute and chronic eosinophilic bronchitis, acute and chronic eosinophilic pneumonia, Churg-Strauss syndrome, hypereosinophilic syndrome, pulmonary eosinophilia induced by drugs, irritant compounds and radiation, pulmonary eosinophilia induced by infection (fungi, tuberculosis, parasites), autoimmunity-related pulmonary eosinophilia, eosinophilic esophagitis, Crohn's disease, or a combination thereof.

69. Method according to claim 49, characterized in that the pulmonary disease or disorder is asthma.

70. Method according to claim 49, characterized in that the pulmonary disease or disorder is chronic obstructive pulmonary disease.