Manufacturing process, tools and methods for MASP-2 inhibitory antibody with low viscosity and high concentration

Abstract

The present invention relates to compositions of MASP-2 inhibitory antibodies with low viscosity and high concentration, kits comprising the compositions and methods of treatment using the compositions and kits to inhibit the deleterious effects of MASP-2-mediated antibody activation.

Description

HIGHLY CONCENTRATED LOW VISCOSITY MASP-2 INHIBITORY ANTIBODY FORMULATIONS, KITS, AND METHODS Cross-Reference to Related ApplicationS This application claims the benefit of US Provisional Application No. 62 / 382,156, filed August 31, 2016, which is hereby incorporated by reference in its entirety. FIELD OF THE INVENTION The present invention relates to stable, high-concentration low-viscosity formulations of MASP-2 inhibitory antibodies, kits comprising the formulations and therapeutic methods using the formulations and kits for inhibiting the adverse effects of MASP-2 dependent complement activation. STATEMENT REGARDING SEQUENCE LISTING The sequence listing associated with this application is provided in text format in lieu of a paper copy and is hereby incorporated by reference into the specification. The name of the text file containing the sequence listing is MP_1_0261_PCT_SequenceListing_20170809_ST25. The text file is 17 KB; was created on August 9, 2017; and is being submitted via EFS-Web with the filing of the specification. BACKGROUND Antibody-based therapy is usually administered on a regular basis and often requires several mg / kg dosing by injection. A preferred form of delivery for treating chronic conditions is outpatient administration of high-dose monoclonal antibodies (several mg per kg) via subcutaneous (SC) injection (Stockwin and Holmes, Expert Opin Biol Ther 3:1133-1152 (2003); Shire et al., J Pharm Sci 93:1390-1402 (2004)). Highly concentrated pharmaceutical formulations of a therapeutic antibody are desirable because they allow lower volume administration and / or fewer administrations which consequently mean less discomfort to the patient. Additionally, such lower volumes allow packaging of the therapeutic doses of a monoclonal antibody in individual single-dose, pre-filled syringes for self-administration. SC delivery via pre-filled syringe or auto-injector technology allows for home administration and improved patient compliance of drug administration. However, the development of a formulation with a high protein concentration poses challenges related to the physical and chemical stability of the protein, as well as difficulty with manufacture, storage and delivery of the protein formulation (see e.g., Wang et al., J of Pharm Sci vol 96(1):1-26, (2007)). A challenge in the development of high protein concentration formulations is concentration-dependent solution viscosity. At a given protein concentration, viscosity varies dramatically as a function of the formulation. In particular, monoclonal antibodies are known to exhibit peculiar and diverse viscosity-concentration profiles that reveal a sharp exponential increase in solution viscosity with increasing monoclonal antibody concentration (see e.g., Connolly B.D. et al., Biophysical Journal vol 103:69-78, (2012)). Another challenge with liquid formulations at high monoclonal antibody concentration is protein physical stability (Alford et al., J.Pharm Sci 97:3005-3021 (2008); Salinas et al., J Pharm Sci 99:82-93 (2010); Sukumar et al., Pharm Res 21:1087-1093 (2004)). Therefore, the high viscosity of monoclonal antibody pharmaceutical formulations at high concentrations together with the potential for decreased stability can impede their development as products suitable for subcutaneous and / or intravenous delivery. The complement system plays a role in the inflammatory response and becomes activated as a result of tissue damage or microbial infection. Complement activation must be tightly regulated to ensure selective targeting of invading microorganisms and avoid self-inflicted damage (Ricklin et al ., Nat. Immunol . 11:785-797, 2010). Currently, it is widely accepted that the complement system can be activated through three distinct pathways: the classical pathway, the lectin pathway, and the alternative pathway. The classical pathway is usually triggered by a complex composed of host antibodies bound to a foreign particle ( i.e ., an antigen) and generally requires prior exposure to an antigen for the generation of a specific antibody response. Since activation of the classical pathway depends on a prior adaptive immune response by the host, the classical pathway is part of the acquired immune system.In contrast, both the lectin and alternative pathways are independent of adaptive immunity and are part of the innate immune system. Mannan-binding lectin-associated serine protease-2 (MASP-2) has been shown to be required for the function of the lectin pathway, one of the principal complement activation pathways (Vorup-Jensen et al., J. Immunol 165:2093-2100, 2000; Ambrus et al., J Immunol . 170:1374-1382, 2003; Schwaeble et al., PNAS 108:7523-7528, 2011). Importantly, inhibition of MASP-2 does not appear to interfere with the antibody-dependent classical complement activation pathway, which is a critical component of the acquired immune response to infection. As described in U.S. Patent No. 9,011,860 (assigned to Omeros corporation), which is hereby incorporated by reference, OMS646, a fully human monoclonal antibody targeting human MASP-2 has been generated which binds to human MASP-2 with high affinity and blocks the lectin pathway complement activity and is therefore useful to treat various lectin complement pathway-associated diseases and disorders. As further described in U.S. Patent No. 7,919,094, U.S. Patent No. 8,840,893, U.S. Patent No.8,652,477, U.S. Patent No. 8,951,522, U.S. Patent No. 9,011,860; U.S. Patent No. 9,644,035, U.S. Patent Application Publication Nos. US2013 / 0344073, US2013 / 0266560, US 2015 / 0166675; US2017 / 0189525; and co-pending U.S. Patent Application Serial Nos. 15 / 476,154, 15 / 347,434, 15 / 470,647, 62 / 315,857, 62 / 275,025 and 62 / 527,926 (each of which is assigned to Omeros Corporation, the assignee of the instant application, each of which is hereby incorporated by reference), MASP-2-dependent complement activation has been implicated as contributing to the pathogenesis of numerous acute and chronic disease states. Therefore, a need exists for a stable, high-concentration, low-viscosity formulation of a MASP-2 monoclonal antibody that is suitable for parenteral (e.g., subcutaneous) administration, for treatment of subject suffering from MASP-2 complement pathway-associated diseases and disorders. SUMMARY In one aspect, the present disclosure provides a stable pharmaceutical formulation suitable for parenteral administration to a mammalian subject, comprising: (a) an aqueous solution comprising a buffer system having a pH of 5.0 to 7.0; and (b) a monoclonal antibody or fragment thereof that specifically binds to human MASP-2 at a concentration of about 50 mg / mL to about 250 mg / mL, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising CDR-H1, CDR-H2 and CDR-H3 of SEQ ID NO:2 and (ii) a light chain variable region comprising CDR-L1, CDR-L2 and CDR-L3 of SEQ ID NO:3, or a variant thereof comprising a heavy chain variable region having at least 95% identity to SEQ ID NO:2 and a light chain variable region having at least 95% identity to SEQ ID NO:3; wherein the formulation has a viscosity of between 2 and 50 centipoise (cP), and wherein the formulation is stable when stored at between 2oC and 8oC for at least one month.In some embodiments, the concentration of the antibody in the formulation is from about 150 mg / mL to about 200 mg / mL. In some embodiments, the viscosity of the formulation less than 25 cP. In some embodiments, the buffering system comprises histidine. In some embodiments, the buffering system comprises citrate. In some embodiments, the formulation further comprises an excipient, such as a tonicity modifying agent in a sufficient amount for the formulation to be hypertonic. In some embodiments, the formulation further comprises a surfactant. In some embodiments, the formulation further comprises a hyaluronidase enzyme in an amount effective to increase the dispersion and / or absorption of the antibody following subcutaneous administration. In another aspect, the formulation is contained within a subcutaneous administration device, such as a pre-filled syringe. In another aspect, the present disclosure provides a kit comprising a pre-filled container containing the formulation. In another aspect, the present disclosure provides a pharmaceutical composition for use in treating a patient suffering from, or at risk for developing a MASP-2-dependent disease or condition, wherein the composition is a sterile, single-use dosage form comprising from about 350 mg to about 400 mg (i.e., 350 mg, 360 mg, 370 mg, 380 mg, 390 mg, or 400 mg) of MASP-2 inhibitory antibody, wherein the composition comprises about 1.8 mL to about 2.2 mL (i.e., 1.8 mL, 1.9mL, 2.0 mL, 2.1 mL or 2.2 mL) of a 185 mg / mL antibody formulation, such as disclosed herein, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and (ii) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3; and wherein the formulation is stable when stored at between 2oC and 8oC for at least six months.In some embodiments, the MASP-2 dependent disease or condition is selected from the group consisting of aHUS, HSCT-TMA, IgAN and Lupus Nephritis (LN). In another aspect, the present disclosure provides a method of treating a subject suffering from a disease or disorder amenable to treatment with a MASP-2 inhibitory antibody comprising administering the formulation comprising a MASP-2 antibody, as disclosed herein. DESCRIPTION OF THE DRAWINGS The foregoing aspects and many of the attendant advantages of this invention will become more readily appreciated as the same become better understood by reference to the following detailed description, when taken in conjunction with the accompanying drawings, wherein: FIGURE 1A graphically illustrates the amount of lectin pathway-dependent membrane attack complex (MAC) deposition in the presence of different amounts of human MASP-2 monoclonal antibody (OMS646), demonstrating that OMS646 inhibits lectin-mediated MAC deposition with an IC50value of approximately 1 nM, as described in Example 1; FIGURE 1B graphically illustrates the amount of classical pathway-dependent MAC deposition in the presence of different amounts of human MASP-2 monoclonal antibody (OMS646), demonstrating that OMS646 does not inhibit classical pathway-mediated MAC deposition, as described in Example 1; FIGURE 1C graphically illustrates the amount of alternative pathway-dependent MAC deposition in the presence of human MASP-2 monoclonal antibody (OMS646), demonstrating that OMS646 does not inhibit alternative pathway-mediated MAC deposition, as described in Example 1; FIGURE 2A graphically illustrates the results for Dynamic Light Scattering (DLS) analysis for OMS646 formulation excipient screening, showing the overall particle diameter observed for formulations containing various candidate excipients, as described in Example 2; FIGURE 2B graphically illustrates the results for DLS analysis for OMS646 formulation excipient screening, showing the overall polydispersity observed for formulations containing various candidate excipients, as described in Example 2; FIGURE 3 graphically illustrates the results of viscosity analysis of a range of OMS646 concentrations in various formulations as measured at pH 5.0 and pH 6.0, as described in Example 2; FIGURE 4 graphically illustrates the percent protein recovery following buffer-exchange for the OMS646 solubility / viscosity study with various candidate formulations, as described in Example 2; FIGURE 5 graphically illustrates the viscosity (as determined by exponential fit of the viscosity data) versus protein concentration for the OMS646 solubility / viscosity study with various candidate formulations, as described in Example 2; FIGURE 6 graphically illustrates the protein concentration-normalized viscosity data for the viscosity study with various candidate OMS646 formulations, as described in Example 2; FIGURE 7A graphically illustrates the average load (lbf) of three candidate OMS646 formulations in a syringeability study using 27 GA (1.25”), 25GA (1”) and 25GA thin-walled (1”) needles as described in Example 3; and FIGURE 7B graphically illustrates the maximum load (lbf) of three candidate OMS646 formulations in a syringeability study using 27 GA (1.25”), 25GA (1”) and 25GA thin-walled (1”) needles as described in Example 3. DESCRIPTION OF THE SEQUENCE LISTING SEQ ID NO:1 human MASP-2 protein (mature) SEQ ID NO:2: OMS646 heavy chain variable region (VH) polypeptide SEQ ID NO:3: OMS646 light chain variable region (VL) polypeptide SEQ ID NO:4: OMS646 heavy chain IgG4 mutated heavy chain full length polypeptide SEQ ID NO:5: OMS646 light chain full length polypeptide SEQ ID NO:6: DNA encoding OMS646 full length heavy chain polypeptide SEQ ID NO:7: DNA encoding OMS646 full length light chain polypeptide. DETAILED DESCRIPTION I. DEFINITIONS Unless specifically defined herein, all terms used herein have the same meaning as would be understood by those of ordinary skill in the art of the present invention. The following definitions are provided in order to provide clarity with respect to the terms as they are used in the specification and claims to describe the present invention. Standard techniques may be used for recombinant DNA, oligonucleotide synthesis, and tissue culture and transformation ( e.g. , electroporation, lipofection). Enzymatic reactions and purification techniques may be performed according to manufacturer's specifications or as commonly accomplished in the art or as described herein. These and related techniques and procedures may be generally performed according to conventional methods well known in the art and as described in various general and more specific references that are cited and discussed throughout the present specification. See e.g. , Sambrook et al. , 2001, MOLECULAR CLONING: A LABORATORY MANUAL, 3d ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; Current Protocols in Molecular Biology (Greene Publ. Assoc. Inc. & John Wiley & Sons, Inc., NY, NY); Current Protocols in Immunology (Edited by: John E. Coligan, Ada M. Kruisbeek, David H. Margulies, Ethan M.Shevach, Warren Strober 2001 John Wiley & Sons, NY, NY); or other relevant Current Protocol publications and other like references. Unless specific definitions are provided, the nomenclature utilized in connection with, and the laboratory procedures and techniques of, molecular biology, analytical chemistry, synthetic organic chemistry, and medicinal and pharmaceutical chemistry described herein are those well known and commonly used in the art. Standard techniques may be used for recombinant technology, molecular biological, microbiological, chemical syntheses, chemical analyses, pharmaceutical preparation, formulation, and delivery, and treatment of patients. The term “pharmaceutical formulation” refers to a preparation that is in such form as to permit the biological activity of the active agent (e.g., MASP-2 inhibitory antibody) to be effective for treatment, and which contains no additional components that are unacceptably toxic to a subject in which the formulation would be administered. Such formulations are sterile. In one embodiment, the pharmaceutical formulation is suitable for parenteral administration, such as subcutaneous administration. The term “MASP-2” refers to mannan-binding lectin-associated serine protease-2. Human MASP-2 protein (mature) is set forth as SEQ ID NO:1. The term "MASP - 2 - dependent complement activation" comprises MASP - 2-dependent activation of the lectin pathway, which occurs under physiological conditions (i.e., in the presence of Ca++) leading to the formation of the lectin pathway C3 convertase C4b2a and upon accumulation of the C3 cleavage product C3b subsequently to the C5 convertase C4b2a(C3b)n. The term "lectin pathway" refers to complement activation that occurs via the specific binding of serum and non - serum carbohydrate - binding proteins including mannan - binding lectin (MBL), CL-11 and the ficolins (H-ficolin, M-ficolin, or L-ficolin). The term "classical pathway" refers to complement activation that is triggered by an antibody bound to a foreign particle and requires binding of the recognition molecule C1q. The term "MASP - 2 inhibitory antibody" refers to an antibody, or antigen binding fragment thereof, that binds to MASP - 2 and effectively inhibits MASP - 2 - dependent complement activation (e.g., OMS646). MASP - 2 inhibitory antibodies useful in the method of the invention may reduce MASP - 2 - dependent complement activation by greater than 20%, such as greater than 30%, or greater than 40%, or greater than 50%, or greater than 60%, or greater than 70%, or greater than 80%, or greater than 90%, or greater than 95%. The term "OMS646 monoclonal antibody" refers to a monoclonal antibody comprising CDR-H1, CDR-H2 and CDR-H3 of the heavy chain variable region amino acid sequence set forth in SEQ ID NO:2 and comprising CDR-L1, CDR-L2 and CDR-L3 of the light chain variable region amino acid sequence set forth in SEQ ID NO:3. This particular antibody is an example of a MASP-2 inhibitory antibody that specifically binds to MASP-2 and inhibits MASP-2 dependent complement activation. A “monoclonal antibody" refers to a homogeneous antibody population wherein the monoclonal antibody is comprised of amino acids (naturally occurring and non-naturally occurring) that are involved in the selective binding of an epitope. Monoclonal antibodies are highly specific for the target antigen . The term "monoclonal antibody" encompasses not only intact monoclonal antibodies and full-length monoclonal antibodies, but also fragments thereof (such as Fab, Fab', F(ab')2, Fv), single chain ( s cFv), variants thereof, fusion proteins comprising an antigen-binding portion, humanized monoclonal antibodies, chimeric monoclonal antibodies, and any other modified configuration of the immunoglobulin molecule that comprises an antigen-binding fragment (epitope recognition site) of the required specificity and the ability to bind to an epitope. It is not intended to be limited as regards the source of the antibody or the manner in which it is made ( e.g., by hybridoma, phage selection, recombinant expression, transgenic animals, etc.). The term includes whole immunoglobulins as well as the fragments etc. described above under the definition of "antibody". T he term "antibody fragment" refers to a portion derived from or related to a full - length antibody, such as, for example, a MASP-2 inhibitory antibody, generally including the antigen binding or variable region thereof. Illustrative examples of antibody fragments include Fab, Fab', F(ab) 2 , F(ab') 2 and Fv fragments, scFv fragments, diabodies, linear antibodies, single - chain antibody molecules and multispecific antibodies formed from antibody fragments. As used herein, a "single - chain Fv" or "scFv" antibody fragment comprises the V H and V L domains of an antibody, wherein these domains are present in a single polypeptide chain. Generally, the Fv polypeptide further comprises a polypeptide linker between the V H and V L domains, which enables the scFv to form the desired structure for antigen binding. The term “CDR region” or “CDR” is intended to indicate the hypervariable regions of the heavy and light chains of the immunoglobulin as defined by Kabat et al., 1991 (Kabat, E. A. et al., (1991) Sequences of Proteins of Immunological Interest, 5thEdition and later editions. An antibody typically contains 3 heavy chain CDRs and 3 light chain CDRs. The term CDR or CDRs is used here in order to indicate, according to the case, one of these regions, or several, or even the whole, of these regions which contain the majority of the amino acid residues responsible for the binding by affinity of the antibody for the antigen of the epitope which it recognizes. The term "specific binding" refers to the ability of an antibody to preferentially bind to a particular analyte that is present in a homogeneous mixture of different analytes. In certain embodiments, a specific binding interaction will discriminate between desirable and undesirable analytes in a sample, in some embodiments more than about 10 to 100-fold or more (e.g., more than about 1000- or 10,000-fold). In certain embodiments, the affinity between a capture agent and analyte when they are specifically bound in a capture agent / analyte complex is characterized by a K D (dissociation constant) of less than about 100 nM, or less than about 50 nM, or less than about 25 nM, or less than about 10 nM, or less than about 5 nM, or less than about 1 nM. The term "isolated antibody" refers to an antibody that has been identified and separated and / or recovered and / or purified from a component of its natural environment or cell culture expression system. In preferred embodiments, the antibody will be purified (1) to greater than 95% by weight of antibody and most preferably more than 99% by weight; as determined by a suitable method to measure protein concentration, such as, for example, the Lowry method, or absorbance at OD280, (2) to a degree sufficient to obtain at least 15 residues of N-terminal or internal amino acid sequence by use of a spinning cup sequenator; or (3) to homogeneity by SDS-PAGE under reducing or non-reducing conditions using Coomassie blue or, preferably, silver stain. Typically an isolated antibody for use in the formulations disclosed herein will be prepared by at least one purification step. As used herein, the amino acid residues are abbreviated as follows: alanine (Ala;A), asparagine (Asn;N), aspartic acid (Asp;D), arginine (Arg;R), cysteine (Cys;C), glutamic acid (Glu;E), glutamine (Gln;Q), glycine (Gly;G), histidine (Hush), isoleucine (Ilia), leucine (Lull), lysine (Lys;K), methionine (Met;M), phenylalanine (Phe;F), proline (Pro;P), serine (Ser;S), threonine (Thr;T), tryptophan (Trp;W), tyrosine (Tyr;Y), and valine (Val;V). In the broadest sense, the naturally occurring amino acids can be divided into groups based upon the chemical characteristic of the side chain of the respective amino acids. By "hydrophobic" amino acid is meant either Ile, Leu, Met, Phe, Trp, Tyr, Val, Ala, Cys or Pro. By "hydrophilic" amino acid is meant either Gly, Asn, Gln, Ser, Thr, Asp, Glu, Lys, Arg or His. This grouping of amino acids can be further subclassed as follows. By "uncharged hydrophilic" amino acid is meant either Ser, Thr, Asn or Gln. By "acidic" amino acid is meant either Glu or Asp. By "basic" amino acid is meant either Lys, Arg or His. As used herein the term "conservative amino acid substitution" is illustrated by a substitution among amino acids within each of the following groups: (1) glycine, alanine, valine, leucine, and isoleucine, (2) phenylalanine, tyrosine, and tryptophan, (3) serine and threonine, (4) aspartate and glutamate, (5) glutamine and asparagine, and (6) lysine, arginine and histidine. As used herein, "a subject" includes all mammals, including without limitation, humans, non - human primates, dogs, cats, horses, sheep, goats, cows, rabbits, pigs and rodents. The term “pharmaceutically acceptable” with respect to an excipient in a pharmaceutical formulation means that the excipient is suitable for administration to a human subject. The term “subcutaneous administration” refers to administration of a formulation under all layers of the skin of a subject. The term "buffer" refers to a buffered solution that resists changes in pH by the action of its acid-base conjugate components. The buffer of this invention has a pH in the range from about 4 to about 8; preferably from about 5 to about 7; and most preferably has a pH in the range from about 5.5 to about 6.5. Examples of buffers that will control the pH in this range include acetate (e.g., sodium acetate), succinate (such as sodium succinate), gluconate, histidine, citrate, and other organic acid buffers. A “buffering agent” is a compound that is used to produce buffered solutions. The term “histidine” specifically includes L-histidine unless otherwise specified. The term "isotonic" refers to a formulation that has essentially the same osmotic pressure as human blood. Isotonic formulations will generally have an osmotic pressure from about 250 to about 350 mOsmol / KgH20. Isotonicity can be measured using a vapor pressure or freezing point depression osmometer, for example. The term “hypertonic” refers to a formulation with an osmotic pressure above that of human (i.e., greater than 350 mOsm / KgH20). The term “tonicity modifying agent” refers to a pharmaceutically acceptable agent suitable to provide an isotonic, or in some embodiments, a hypertonic formulation. The term “sterile” refers to a pharmaceutical product that is asceptic or free of viable bacteria, fungi or other microorganisms, which can be achieved by any suitable means, such as, for example, a formulation that has been aseptically processed and filled, or filtered through sterile filtration membranes, prior to, or following, preparation of the formulation and filled. The term “stable formulation” refers to maintenance of the starting level of purity of a formulation over a period of time. In other words, if a formulation is at least 95% pure, such as at least 96% pure, at least 97% pure, at least 98% pure or at least 99% pure with respect to a given antibody species (e.g., MASP-2 inhibitory antibody) at time 0, stability is a measure of how well and for how long the formulation retains substantially this level of purity (e.g., without formation of other species, such as fragmented portions (LMW) or aggregates of the pure species (HMW)). A formulation is stable if the level of purity does not decrease substantially when stored at approximately 2-8ºC over a given period of time, such as at least 6 months, at least 9 months, at least 12 months, or at least 24 months.By “not decrease substantially,” is meant that the level of purity of the formulation changes by less than 5%, such as by less than 4%, or by less than 3%, or by less than 2% or by less than 1% per time period (e.g., over 6 months, over 9 months or over 12 months or over 24 months). In one embodiment, a stable formulation is stable at a temperature of from 2-8ºC for a period of at least six months. In a preferred embodiment, a stable formulation is stable at a temperature of from 2-8ºC for a period of at least one year, or for a period of at least two years. In one embodiment, the formulation is stable if the MASP-2 inhibitory antibody remains at least 95% monomeric during storage at 2°C to 8°C for at least one month, or for at least six months, or for at least 12 months, as determined by SEC-HPLC. The term "preservative" refers to a compound which can be included in a formulation to essentially reduce bacterial growth or contamination. Non-limiting examples of potential preservatives include octadecyldimethylbenzyl ammonium chloride, hexamethonium chloride, benzalkonium chloride (a mixture of alkylbenzyldimethylammonium chlorides in which the alkyl groups are long-chain compounds), and benzethonium chloride. Other types of preservatives include aromatic alcohols such as phenol, butyl and benzyl alcohol, alkyl parabens such as methyl or propyl paraben, catechol, resorcinol, cyclohexanol, 3-pentanol, and m-cresol. The term “excipient” refers to an inert substance in a formulation which imparts a beneficial physical property to a formulation such as increased protein stability and / or decreased viscosity. Examples of suitable excipients include, but are not limited to, proteins (e.g., serum albumin), amino acids (e.g., aspartic acid, glutamic acid, lysine arginine, glycine and histidine), saccharides (e.g., glucose, sucrose, maltose and trehalose), polyols (e.g., mannitol and sorbitol), fatty acids and phospholipids (e.g., alkyl sulfonates and caprylate). The term "substantially free" means that either no substance is present or only minimal, trace amounts of the substance are present which do not have any substantial impact on the properties of the composition. If reference is made to no amount of a substance, it should be understood as "no detectable amount.” The term “viscosity” refers to the measure of the resistance of a fluid which is being deformed by either shear stress or tensile stress; it can be evaluated using a viscometer (e.g., a rolling ball viscometer) or rheometer. Unless otherwise indicated, the viscosity measurement (centipoise, cP) is that at about 25°C with a shear rate in the range of 100,000 to 250,000 1 / sec. The term “parenteral administration” refers to a route of administration other than by way of the intestines and includes injection of a dosage form into the body by a syringe or other mechanical device such as an infusion pump. Parenteral routes can include intravenous, intramuscular, subcutaneous and intraperitoneal routes of administration . Subcutaneous injection is a preferred route of administration. The term "treatment" refers to therapeutic treatment and / or prophylactic or preventative measures. Those in need of treatment include the subjects already having the disease as well as those in which the disease is to be prevented. Hence, the patient to be treated herein may have been diagnosed as having the disease or may be predisposed or susceptible to the disease. The term "effective amount" refers to an amount of a substance that provides the desired effect. In the case of a pharmaceutical drug substance it is the amount of active ingredient effective to treat a disease in the patient. In the case of a formulation ingredient, for example, a hyaluronidase enzyme, an effective amount is the amount necessary to increase the dispersion and absorption of the co-administered MASP-2 inhibitory antibody in such a way that the MASP-2 inhibitory antibody can act in a therapeutically effective way as outlined above. As used herein, the term “about” as used herein is meant to specify that the specific value provided may vary to a certain extent, such as a variation in the range of ±10%, preferably ±5%, most preferably ±2% are included in the given value. For example, the phrase “a pharmaceutical formulation having about 200 mg / mL MASP-2 inhibitory antibody” is understood to mean that the formulation can have from 180 mg / mL to 220 mg / mL MASP-2 inhibitory antibody (e.g., OMS646). Where ranges are stated, the endpoints are included within the range unless otherwise stated or otherwise evident from the context. As used herein the singular forms "a", "an" and "the" include plural aspects unless the context clearly dictates otherwise. Thus, for example, reference to "an excipient" includes a plurality of such excipients and equivalents thereof known to those skilled in the art, reference to "an agent" includes one agent, as well as two or more agents; reference to "an antibody" includes a plurality of such antibodies and reference to "a framework region" includes reference to one or more framework regions and equivalents thereof known to those skilled in the art, and so forth. Each embodiment in this specification is to be applied mutatis mutandis to every other embodiment unless expressly stated otherwise. It is contemplated that any embodiment discussed in this specification can be implemented with respect to any method, kit, reagent, or composition of the invention, and vice versa. Furthermore, compositions of the invention can be used to achieve methods of the invention. II. Overview of the Invention The present disclosure provides stable, high-concentration low-viscosity MASP-2 inhibitory antibody pharmaceutical formulations suitable for parenteral administration (e.g., subcutaneous administration) and also suitable for dilution prior to intravenous administration. Highly concentrated pharmaceutical formulations of therapeutic antibody are desirable because they allow lower volume administration and / or fewer administrations, which consequently mean less discomfort to the patient. Additionally, such lower volumes allow packaging of the therapeutic doses of MASP-2 inhibitory antibody in individual single-dose, pre-filled syringes or vials for self-administration. The high-concentration, low-viscosity formulations of the present disclosure comprise an aqueous solution comprising a buffer system having a pH of 4.0 to 8.0, more preferably having a pH of about 5.0 to about 7.0, and a MASP-2 inhibitory monoclonal antibody (e.g., OMS646) or antigen-binding fragment thereof at a concentration of about 50 mg / mL to about 250 mg / mL. In preferred embodiments, the MASP-2 inhibitory antibody (e.g., OMS646) is present in the high concentration formulations suitable for subcutaneous administration at a concentration of from about 100 mg / mL to about 250 mg / mL. In particular embodiments, the MASP-2 inhibitory antibody (e.g., OMS646) is present in the high concentration formulations at a concentration of from about 150 mg / mL to about 200 mg / mL, such as about 175 mg / mL to about 195 mg / mL, such as about 185 mg / mL. In various embodiments, the pharmaceutical formulations further comprise, in addition to the highly concentration MASP-2 inhibitory antibody and buffer system, one or more excipients, such as a tonicity modifying agent (e.g., an amino acid with a charged side chain), and optionally a non-ionic surfactant. In some embodiments, the pharmaceutical formulations in accordance with this disclosure further comprise a hyaluronidase enzyme. A significant advantage of the highly concentrated pharmaceutical formulations of MASP-2 inhibitory antibody of the present invention is their low viscosity at high protein concentrations. As known to those skilled in the art, high viscosity of monoclonal antibody pharmaceutical formulations at concentrations ≥100 mg / mL can impede their development as products suitable for subcutaneous and / or intravenous delivery. Therefore, pharmaceutical formulations having lower viscosity are highly desirable because of their ease of manufacturability, such as but not limited to processing, filtering, and filling.As described in Examples 2 and 3 herein, the formulations of the present disclosure comprising from 100 mg / mL to 200 mg / mL MASP-2 inhibitory antibody OMS646 have surprisingly low viscosity, such as a viscosity less than about 50 cP, such as between 2 cP and 50 cP, such as between 2 cP and 40 cP, such as between 2 cP and 30 cP, or between 2 cP and 25 cP, or between 2 cP and 20 cP, or between 2 cP and 18 cP. Additionally, the low viscosity, highly concentrated MASP-2 inhibitory antibody pharmaceutical formulations of the present invention allow the pharmaceutical formulations to be administered via standard syringe and needles, auto-injector devices, and microinfusion devices known in the art. As described in Example 3, the high concentration low viscosity of the MASP-2 inhibitory antibody pharmaceutical formulations as disclosed herein were determined to have syringeability and injectability suitable for subcutaneous administration. Syringeability and injectability are key product performance parameters of a pharmaceutical formulation intended for any parenteral administration, e.g., intramuscular or subcutaneous and permit the administration of such formulations by intramuscular or subcutaneous injection via small-bore needles typically used for such injections, such as, for example, 29GA regular or thin-walled, 27GA (1.25”) regular or thin-walled, or 25GA (1”) regular or thin-walled needles. In some instances, the low viscosity of MASP-2 inhibitory antibody pharmaceutical formulations as disclosed herein permit the administration of an acceptable (for example, 1-3 cc) injected volume while delivering an effective amount of the MASP-2 inhibitory antibody OMS646 in a single injection at a single injection site. A further significant advantage of the formulations of the present disclosure is that the high concentration low viscosity formulations of MASP-2 inhibitory antibody (i.e., ≥100 mg / mL to 200 mg / mL) are stable when stored at 2°C to 8° C for at least 30 days, up to at least 9 months, or up to at least 12 months or longer, as described in the stability studies in Examples 2 and 4. The present disclosure also provides a process for the preparation of the high concentration low viscosity MASP-2 inhibitory antibody formulations, containers including said formulations, therapeutic kits comprising the formulations; and to therapeutic methods of using such formulation, containers and kits for the treatment of a subject suffering from, or at risk for developing a disease or condition associated with MASP-2-dependent complement activation. MASP-2 Inhibitory Antibody As detailed herein, the present invention is drawn to formulations comprising monoclonal antibodies that specifically bind to MASP-2 and inhibit MASP-2-dependent complement activation and antigen-binding fragments thereof. In certain embodiments, a MASP-2 inhibitory antibody or antigen-binding fragment thereof for use in the claimed formulations is a MASP-2 inhibitory antibody referred to as “OMS646” as described in WO2012 / 151481 (hereby incorporated herein by reference) which comprises a heavy chain polypeptide comprising the amino acid sequence of SEQ ID NO:2 and a light chain polypeptide comprising the amino acid sequence of SEQ ID NO:3. As described in WO2012 / 151481 and described in Example 1, OMS646 specifically binds to human MASP-2 with high affinity and has the ability to block lectin pathway complement activity. In certain embodiments,a MASP-2 inhibitory antibody or antigen-binding fragment thereof for use in the claimed formulations is a MASP-2 inhibitory antibody comprising a heavy-chain variable region comprising (i) CDR-H1 comprising the amino acid sequence from 31-35 of SEQ ID NO:2, (ii) CDR-H2 comprising the amino acid sequence from 50-65 of SEQ ID NO:2, and iii) CDR-H3 comprising the amino acid sequence from 95-107 of SEQ ID NO:2; and (b) a light-chain variable region comprising: i) CDR-L1 comprising the amino acid sequence from 24-34 of SEQ ID NO:3, ii) CDR-L2 comprising the amino acid sequence from 50-56 of SEQ ID NO:3, and iii) CDR-L3 comprising the amino acid sequence from 89-97 of SEQ ID NO:3. In some embodiments, the MASP-2 inhibitory antibody for use in the claimed formulations comprises a variant of OMS646 comprising a heavy chain variable region having at least 95% identity to SEQ ID NO:2 and comprising a light chain variable region having at least 95% identity to SEQ ID NO:3. In some embodiments,the MASP-2 inhibitory antibody for use in the claimed formulations comprises a variant of OMS646 comprising an amino acid sequence having at least 95% identity to SEQ ID NO:2, wherein residue 31 is an R, residue 32 is a G, residue 33 is a K, residue 34 is an M, residue 35 is a G, residue 36 is a V, residue 37 is an S, residue 50 is an L, residue 51 is an A , residue 52 is an H, residue 53 is an I, residue 54 is an F, residue 55 is an S, residue 56 is an S, residue 57 is a D, residue 58 is an E, residue 59 is a K, residue 60 is an S, residue 61 is a Y, residue 62 is an R, residue 63 is a T, residue 64 is an S, residue 65 is an L, residue 66 is a K, residue 67 is an S, residue 95 is a Y, residue 96 is a Y, residue 97 is a C, residue 98 is an A, residue 99 is an R, residue 100 is an I, residue 101 is an R, residue 102 is an R or A, residue 103 is a G, residue 104 is a G, residue 105 is an I,residue 106 is a D and residue 107 is a Y; and b) a light chain variable region comprising an amino acid sequence having at least 95% identity to SEQ ID NO:3, wherein residue 23 is an S, residue 24 is a G, residue 25 is an E or D, residue 26 is a K, residue 27 is an L, residue 28 is a G, residue 29 is a D, residue 30 is a K, residue 31 is a Y or F, residue 32 is an A, residue 33 is a Y, residue 49 is a Q, residue 50 is a D, residue 51 is a K or N, residue 52 is a Q or K, residue 53 is an R, residue 54 is a P, residue 55 is an S, residue 56 is a G, residue 88 is a Q, residue 89 is an A, residue 90 is a W, residue 91 is a D, residue 92 is an S, residue 93 is an S, residue 94 is a T, residue 95 is an A, residue 96 is a V and residue 97 is an F., In some embodiments, the monoclonal MASP-2 inhibitory antibody (e.g., OMS646 or a variant thereof) for use in the claimed formulations is a full length monoclonal antibody. In some embodiments, the monoclonal MASP-2 inhibitory antibody is a human IgG4 full length antibody. In some embodiments, the IgG4 comprises a point mutation in the hinge region to enhance the stability of the antibody. In some embodiments, the MASP-2 inhibitory antibody (e.g., OMS646 or a variant thereof) is comprised of variable regions of human origin fused to human IgG4 heavy chain and lambda light chain constant regions, wherein the heavy chain comprises a point mutation in the hinge region (e.g., wherein the IgG4 molecule comprises a S228P mutation) to enhance the stability of the antibody. In some embodiments, the MASP-2 inhibitory antibody is a tetramer consisting of two identical heavy chains having the amino acid sequence set forth in SEQ ID NO:4 and two identical light chains having the amino acid sequence set forth in SEQ ID NO:5. In some embodiments, the concentration of the MASP-2 inhibitory antibody in the formulation is from about 100 mg / mL to about 250 mg / mL, such as about 150 mg / ml to about 220 mg / mL, such as about 175 mg / mL to about 200 mg / mL, or about 175 mg / mL to about 195 mg / mL. In certain embodiments, the MASP-2 inhibitory antibody is present in the formulation at a concentration of about 175 mg / ml to about 195 mg / ml, such as about 180 mg / mL to about 190 mg / mL, such as about 175 mg / mL, such as about 180 mg / mL, about 181 mg / mL, about 182 mg / mL, about 183 mg / mL, about 184 mg / mL, about 185 mg / mL, about 186 mg / mL, about 187 mg / mL, about 188 mg / mL, about 189 mg / mL or such as about 190 mg / mL. In some embodiments, minor variations in the amino acid sequences of the MASP-2 inhibitory antibodies or fragments thereof are contemplated as being encompassed by the claimed formulations, provided that the variations in the amino acid sequence maintains at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to the MASP-2 inhibitory antibodies or antigen-binding fragments thereof described herein (i.e., at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to SEQ ID NO:2 and / or at least at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity to SEQ ID NO:3) and retain the ability to inhibit MASP-2-dependent complement activation. As will be appreciated, MASP-2 inhibitory antibodies or antigen-binding fragments thereof that are formulated in the context of the present disclosure can be produced using techniques well known in the art (e.g., recombinant technologies, phage display technologies, synthetic technologies, or combinations of such technologies or other technologies readily known in the art). Methods for producing and purifying antibodies and antigen-binding fragments are well known in the art and can be found, for example, in Harlow and Lane (1988) Antibodies, A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, Chapters 5-8 and 15. For example, MASP-2 inhibitory antibodies, such as OMS646 can be expressed in a suitable mammalian cell line. Sequences encoding the heavy chain variable region and the light chain variable region of a particular antibody of interest such as OMS646 (e.g., SEQ ID NO:6 and SEQ ID NO:7) can be used to transform a suitable mammalian host cell. Methods for introducing heterologous polynucleotides into mammalian cells are well known in the art and include dextran-mediated transfection, calcium phosphate precipitation, polybrene mediated transfection, protoplast fusion, electroporation, encapsulation of the polynucleotide(s) in liposomes, and direct microinjection of the DNA into nuclei. Mammalian cell lines available as hosts for expression are well known in the art and include many immortalized cell lines available from the American Type Culture Collection (ATCC), including but not limited to Chinese hamster ovary (CHO) cells, HeLa cells, baby hamster kidney (BNK) cells, monkey kidney cells (COS), human hepatocellular carcinoma cells (e.g., HepG2), human epithelial kidney 293 cells (HEK293) and numerous other cell lines. Following the protein production phase of the cell culture process, MASP-2 inhibitory antibodies are recovered from the cell culture medium using techniques understood by one skilled in the art. In particular, in some embodiments the MASP-2 inhibitory antibody heavy and light chain polypeptides are recovered from the culture medium as secreted polypeptides. MASP-2 inhibitory antibodies can be purified using, for example, hydroxyapatite chromatography, gel electrophoresis, dialysis, and affinity chromatography, and any combination of known or yet to be discovered purification techniques, including but not limited to Protein A chromatography, fractionation on an ion-exchange column, ethanol precipitation, reverse phase HPLC, chromatography on silica, chromatography on heparin SEPHAROSET®, an anion or cation exchange resin chromatography (such as a polyaspartic acid column), chromatofocusing, SDS- PAGE, and ammonium sulfate precipitation. The purification method can further comprise additional steps that inactivate and / or remove viruses and / or retroviruses that might potentially be present in the cell culture medium of mammalian cell lines.A significant number of viral clearance steps are available, including but not limited to, treating with chaotropes such as urea or guanidine, detergents, additional ultrafiltration / diafiltration steps, conventional separation, such as ion-exchange or size exclusion chromatography, pH extremes, heat, proteases, organic solvents or any combination thereof. The purified MASP-2 inhibitory antibodies typically require concentration and a buffer exchange prior to storage or further processing. As a non-limiting example, a tangential flow filtration (TFF) system may be used to concentrate and exchange the elution buffer from the previous purification column with the final buffer desired for the drug substance. The monoclonal MASP-2 inhibitory antibody which is formulated herein is preferably essentially pure and desirably essentially homogeneous (i.e., free from contaminating proteins, etc.). “Essentially pure” antibody means a composition comprising at least 90% by weight of the antibody, based on the total weight of the composition, preferably at least 95% by weight. “Essentially homogenous” antibody means a composition comprising at least about 99% by weight of antibody, based on total weight of the composition. Aqueous Solutions The high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure comprises an aqueous solution comprising a buffer system having a pH of 4.0 to 8.0 (e.g., having a pH from about 5.0 to about 7.0, or having a pH from about 5.5 to about 6.5) and a MASP-2 inhibitory antibody (e.g., OMS646 or a variant thereof) or antigen-binding fragment thereof at a concentration of about 50 mg / mL to about 250 mg / mL (e.g., from about 100mg / mL to about 250 mg / mL). The aqueous solution for use in the formulations of the present disclosure is one which is pharmaceutically acceptable (safe and non-toxic for administration to a human) and is useful for the preparation of a liquid formulation. In some embodiments, the aqueous solution is water, such as sterile water for injection (WFI), which is a sterile, solute-free preparation of distilled water.Alternatively, other aqueous solutions that are suitable for therapeutic administration and which would not adversely affect the stability of the formulation may be used, such as deionized water. Other suitable aqueous solutions include bacteriostatic water for injection (BWFI), sterile saline solution, Ringer’s solution, or other similar aqueous solutions used for pharmaceutical solutions. Buffering Systems The high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure is adjusted to a pH from 4.0 to 8.0, preferably from pH 5.0 to 7.0. The desired pH is suitably maintained by use of a buffering system. In some embodiments, the buffer system comprises at least one pharmaceutically acceptable buffering agent with an acid dissociation constant within 2 pH units of the formulation pH. The buffer system used in the formulations in accordance with the present invention has a pH in the range from about 4.0 to about 8.0. Various buffering agents are known to the person skilled in the art. Examples of buffering agents that will control the pH in this range include acetate, succinate, gluconate, histidine, citrate, and other organic acid buffers. In some embodiments, the buffering agent is selected from the group consisting of succinate, histidine and citrate.In some embodiments, the pharmaceutical formulations comprise a buffering system with a buffering agent in a concentration of from 1 to 50 mM, such as from 10 to 40 mM, or such as from 10 to 30 mM, or from 20 to 30mM, or about 20 mM. In some embodiments, the buffering agent is a histidine buffer. A “histidine buffer” is a buffer comprising the amino acid histidine. Examples of histidine buffers include histidine or any histidine salts including histidine hydrochloride, histidine acetate, histidine phosphate, and histidine sulfate, including combinations of any of these salts with or without histidine. In one embodiment, the buffering system comprises histidine hydrochloride buffer (L-Histidine / HCL). Such histidine hydrochloride buffer may be prepared by titrating L-histidine (free base, solid) with diluted hydrochloric acid or by using the appropriate mixture of histidine and histidine hydrochloride. In some embodiments, the pH of the L-Histidine / HCl buffer is about 5.0 to about 7.0, such as about 5.5 to about 6.0, e.g., about 5.8 or about 5.9. In some embodiments, the buffering agent is a citrate buffer. Such citrate buffer may be prepared by titrating citric acid, the mono-sodium salt of citric acid, and / or the di-sodium salt of citric acid with diluted sodium hydroxide solution to the appropriate pH or by using the appropriate mixture of citric acid and the salt(s) to achieve this same pH. In another embodiment, the citrate buffer may be prepared by titrating a tri-sodium citrate solution with diluted hydrochloric acid solution to the appropriate pH. In this case, the ionic strength may be slightly higher than starting with citric acid due to the generation of additional ions of sodium and chloride in the solution. In certain embodiments, the pH of the citrate buffer is about 5.0 to about 7.0, such as about 5.5 to about 6.0, e.g., about 5.8 or about 5.9. In some embodiments, the buffering agent is a succinate buffer. In certain embodiments, the pH of the succinate buffer is about 5.5 to about 6.0, e.g., about 5.8 or about 5.9. In some embodiments, the buffering agent is a sodium citrate buffer, wherein sodium citrate is present in the formulation at a concentration of about 10 mM to about 50 mM, such as from about 10 mM to about 25 mM, such as about 20 mM. In some embodiments, the buffering agent is a L-histidine buffer, wherein L-histidine is present in the formulation at a concentration of about 10mM to about 50 mM, such as from about 10 mM to about 25 mM, such as about 20 mM. In some embodiments, the formulation comprises about 20 mM sodium citrate and has a pH from about 5.0 to about 7.0. In some embodiments, the formulation comprises about 20 mM L-histidine and has a pH from about 5.0 to about 7.0. Excipients In some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure further comprises at least one excipient. Examples of suitable excipients include, but are not limited to, proteins (e.g., serum albumin), amino acids (e.g., aspartic acid, glutamic acid, lysine, arginine, glycine and histidine), saccharides (e.g., glucose, sucrose, maltose and trehalose), polyols (e.g., mannitol and sorbitol), fatty acids and phospholipids (e.g., alkyl sulfonates and caprylate). In some embodiments, the formulation comprises an excipient selected from the group consisting of an amino acid with a charged side chain, a sugar or other polyol and a salt. In some embodiments, the formulation comprises a sugar or other polyol, such as, for example, sucrose, trehalose, mannitol or sorbitol. In some embodiments, the formulation comprises a salt, such as, for example NaCl or a salt of an amino acid. In some embodiments, the formulation comprises an excipient that is a tonicity modifying agent. In some embodiments, the tonicity modifying agent is included in the formulation in a concentration suitable to provide an isotonic formulation. In some embodiments, the tonicity modifying agent is included in the formulation in a concentration suitable to provide a hypertonic formulation. In some embodiments, the tonicity modifying agent for use in the formulation is selected from the group consisting of an amino acid with a charged side chain, a sugar or other polyol and a salt. In some embodiments, the tonicity modifying agent is an amino acid with a charged side chain (i.e., a negatively charged side chain or a positively charged side chain) at a concentration of from about 50 mM to about 300 mM. In some embodiments, the tonicity modifying agent is an amino acid with a negatively charged side chain, such as glutamate.In some embodiments, the formulation comprises glutamate at a concentration of about 50mM to about 300 mM. In some embodiments, the tonicity modifying agent is an amino acid with a positively charged side chain, such as arginine. In some embodiments, the formulation comprises arginine (e.g., arginine HCL), at a concentration of from about 50 mM to about 300 mM, such as from about 150 mM to about 225 mM. Preferably, the pharmaceutical formulations as disclosed herein are hypertonic (i.e., have a higher osmotic pressure than human blood). As described herein, it was unexpectedly observed that hypertonicity led to reduced sample viscosity, which was achieved, for example, with modest increases in arginine concentration. As described in Example 2, it was unexpectedly observed that low viscosities were achieved (e.g., less than 25 cP) with the citrate / arginine and the histidine / arginine high concentration MASP-2 inhibitory antibody formulations comprising an arginine concentration of 200 mM or greater in the absence of CaCl2. Accordingly, in some embodiments, the formulation comprises arginine (e.g., arginine HCL) at a hypertonic level of from about 200 mM to about 300 mM. As further described in Example 2, it was also observed that formulations which included divalent cations (CaCl2or MgCl2) had elevated high molecular weight material as compared to formulations that did not include CaCl2or MgCl2additives. Accordingly, in one embodiment, the high-concentration, low viscosity MASP-2 inhibitory antibody formulation of the present disclosure is substantially free of a CaCl2additive. In one embodiment, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure is substantially free of a MgCl2additive. As further described in Example 2, it was determined for the high concentration MASP-2 antibody formulations that the inclusion of sucrose was associated with elevated polydispersity in all buffering systems tested. Accordingly, in one embodiment, the high concentration low viscosity MASP-2 inhibitory antibody formulation of the present disclosure is substantially free of sucrose. As described in Example 2, it was also determined for the high concentration MASP-2 antibody formulations that the inclusion of sorbitol was associated with elevated polydispersity in all buffering systems tested. Accordingly, in one embodiment, the high concentration low viscosity MASP-2 inhibitory antibody formulation of the present disclosure is substantially free of sorbitol. Surfactants Optionally, in some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure further comprises a pharmaceutically acceptable surfactant. Non-limiting examples of suitable pharmaceutically acceptable surfactants include polyoxyethylensorbitan fatty acid esters (e.g., Tween), polyethylene-polypropylene glycols, polyoxyethylene-stearates, polyoxyethylene alkyl ethers (e.g., polyoxyethylene monolauryl ether), alkylphenylpolyoxyethylene ethers (e.g., Triton-X), polyoxyethylene-polyoxypropylene copolymer (e.g., Poloxamer and Pluronic), and sodium dodecyl sulphate (SDS). In certain embodiments, the pharmaceutically acceptable surfactant is a polyoxyethylenesorbitan-fatty acid ester (polysorbate), such as polysorbate 20 (sold under the trademark Tween 20TM) and polysorbate 80 (sold under the trademark Tween 80TM).In some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure comprises a non-ionic surfactant. The nonionic surfactant can be a polysorbate, (e.g., selected from the group of polysorbate 20, polysorbate 80, and polyethylene-polypropylene copolymer). In some embodiments, the concentration of the surfactant is about 0.001 to 0.1% (w / v), or 0.005% to 0.1% (w / v), or 0.01 to 0.1% (w / v), or 0.01 to 0.08% (w / v), or 0.025 to 0.075% (w / v), or more particularly about 0.01% (w / v), about 0.02% (w / v), about 0.04% (w / v), or about 0.06% (w / v), or about 0.08% (w / v), or about 0.10% (w / v). In some embodiments, the formulation comprises a non-ionic surfactant (e.g., polysorbate 80) at a concentration of from about 0.001 to 0.1% (w / v), or 0.005% to 0.1% (w / v), or 0.01 to 0.1% (w / v), or 0.01 to 0.08% (w / v), or 0.025 to 0.075% (w / v), or more particularly about 0.01% (w / v), about 0.02% (w / v), about 0.04% (w / v), or about 0.06% (w / v), or about 0.08% (w / v), or about 0.10% (w / v). As described in Example 2, it was unexpectedly observed that the inclusion of the non-ionic surfactant polysorbate 80 (PS-80) led to a further reduction in viscosity while also preserving protein recovery, thereby allowing for a high concentration of OMS646 antibody while maintaining a low viscosity suitable for use in an injection device, such as an autoinjector. Stabilizers Optionally, in some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure further comprises a stabilizer. The stabilizer (used synonymously with the term "stabilizing agent" herein) may be a carbohydrate or saccharide or a sugar admitted by the regulatory authorities as a suitable additive or excipient in pharmaceutical formulations, e.g., trehalose or sucrose. The typical concentration of the stabilizer is 15 to 250 mM, or 150 to 250 mM, or about 210 mM. The formulations may contain a secondary stabilizer, such as methionine, e.g., in a concentration of 5 to 25 mM or in a concentration of 5 to 15 mM (e.g., methionine in a concentration of about 5 mM, about 10 mM or about 15 mM). Preservatives Optionally, in some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure further comprises a preservative (e.g., an antimicrobial agent). Antimicrobial agents are generally required for parenteral products that are intended for multiple dosing. Similarly, preservatives are added to pharmaceutical formulations aseptically packaged in single dose vials if the active ingredient(s) does not have bactericidal or bacteriostatic properties or is growth promoting. Some typical preservatives used are benzyl alcohol (0.9% to 1.5%), methylparaben (0.18% to 0.2%), propylparaben (0.02%), benzalkonium chloride (0.01% to 0.02%), and thimerosal (0.001% to 0.01%). Syringeability The subcutaneous route of administration requires injections using injection devices, such as syringes, auto-injectors, wearable pumps, or other devices, which restricts product formulation with regard to injection volume and solution viscosity. In addition, product formulation must be suitable for use in an injection device with regard to injection force and time required for injection delivery. “Syringeablity,” as used herein, refers to the ability of an injectable therapeutic to pass easily through a hypodermic needle on transfer from a vial prior to an injection. “Injectability,” as used herein, refers to the performance of the formulation during injection (see, e.g., Cilurzo F, Selmin F, Minghetti P, et al. Injectability Evaluation: An Open Issue. AAPS PharmSciTech . 2011;12(2):604-609). Syringeability includes such factors as ease of withdrawal, clogging and foaming tendencies, and accuracy of dose measurements.Injectability includes pressure or force required for injection, evenness of flow, and freedom from clogging (i.e., no blockage of the syringe needle). Syringeability and injectability can be affected by the needle geometry, i.e., inner diameter, length, shape of the opening, as well as the surface finish of the syringe, especially in self-injection devices such as pens and auto-injectors (e.g., equipped with 29–31 GA needles), and in pre-filled syringes for subcutaneous dosing (e.g., equipped with 24-27 GA needles). Injection force (or glide force) is a complex factor influenced by solution viscosity, the size of the needle (i.e., needle gauge), and surface tension of the container / closure. Smaller needles, e.g., ≥ gauge, will pose less pain sensation to patients. Overcashier and co-workers established a viscosity-glide force relationship as a function of needle gauge based on Hagen-Poiseuille Equation (Overcashier et al., Am Pharm Rev 9(6):77-83 (2006).For example, with a 27-gauge thin walled needle, the liquid viscosity should be maintained at or below 20 cP in order to not exceed the glide force of 25 Newton (N). In certain embodiments, the pharmaceutical formulations of the invention are characterized by having an injection glide force of about 25N or less when injected through a 27GA (1.25”) needle at room temperature. In certain embodiments, the pharmaceutical formulations of the invention are characterized by having an injection glide force of about 20N or less when injected through a 25GA (1”) needle at room temperature. As exemplified in Example 3, the high-concentration, low-viscosity MASP-2 inhibitory antibody (e.g., OMS646) formulations of the present disclosure have surprisingly good syringeability and injectability. The high-concentration, low-viscosity MASP-2 inhibitory antibody formulations as disclosed herein allow for the administration of such formulations by intramuscular or subcutaneous injection via small-bore needles typically used for such injections, for example, 27G (1.25”), 27G thin-walled, 25G thin-walled (1”), or 25G (1”) needles. In some instances, the low viscosity of MASP-2 inhibitory antibody formulations as disclosed herein allows for the administration of a tolerable (for example, 1-3 cc) injected volume while delivering an effective amount of the MASP-2 inhibitory antibody in a single injection at a single injection site. Stability For any of the foregoing, it should be noted that the MASP-2 inhibitory antibody or antigen binding fragment thereof in the formulation retains the ability to inhibit MASP-2-dependent complement activation. For example, the MASP-2 inhibitory antibody retains the ability to bind MASP-2 and inhibit lectin pathway activity as described in Example 1 or other lectin pathway assay, for example as described in WO2012 / 151481. In addition to potency assays, various physical-chemical assays can be used to assess stability including isoelectric focusing, polyacrylamide gel electrophoresis, size exclusion chromatography, and visible and subvisible particle assessment. In certain embodiments, the formulations of the present disclosure exhibit stability at a temperature range of -20°C to 8°C for at least 30 days, up to at least 9 months or longer, or up to at least 12 months or longer, as described in the stability studies in Examples 2 and 4. Additionally or alternatively, in certain embodiments, the formulations are stable at the temperature of -20°C to 8° C, such as from 2°C to 8°C for at least 6 months, at least 1 year, or at least 2 years or longer. In certain embodiments, stability may be assessed, for example, by maintenance of a level of purity over time.For example, in certain embodiments, formulations of the present disclosure have less than 5% decrease, such as less than 4% decrease, such as less than 3% decrease, such as less than 2%, such as less than 1% decrease in purity per month, 6 months, 9 months, or 1 year when stored at 2°C to 8°C, as determined by size exclusion chromatography (SEC), which monitors the presence or absence of fragments (LMW) and / or aggregate species (HMW). In certain embodiments, the formulations of the present disclosure promote low to undetectable levels of aggregation and / or fragmentation and maintain potency after storage for a defined period. Described another way, the formulations disclosed herein are capable of maintaining the structural integrity of the MASP-2 inhibitory antibody OMS646 present at high concentrations in a solution, e.g., at concentrations of greater than 150 mg / mL, or greater than 175 mg / mL, or of at least 185 mg / mL, such that the MASP-2 inhibitory antibody can remain predominately monomeric (i.e., at least 95% or greater) after storage of a defined period at approximately 2°C to 8°C. Preferably, no more than 5%, no more than 4%, no more than 3%, no more than 2%, no more than 1%, and most preferably no more than 0.5% of the antibody forms fragment (LMW) or aggregate forms (HMW) as measured by SEC after storage of a defined period at approximately 2°C to 8°C. As exemplified in Example 4 described herein, the inventors provide formulations suitable for maintaining a MASP-2 inhibitory antibody, OMS646, at about 185 mg / mL in predominately monomeric form for at least 12 months at about 2°C to 8°C. Tissue Permeability Modifier In another embodiment, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulations of the present disclosure further comprise a tissue permeability modifier that increases the absorption or dispersion of the MASP-2 inhibitory antibody following parenteral administration (e.g., subcutaneous injection). In some embodiments, the tissue permeability modifier is a hyaluronidase enzyme which acts as a tissue permeability modifier and increases the dispersion and absorption of the injected MASP-2 inhibitory antibody. A particularly useful tissue permeability modifier is hyaluronidase (e.g., a recombinant human hyaluronidase). Hyaluronidases work as tissue permeability modifiers by temporarily breaking down the hyaluronan barrier to open access to the lymphatic and capillary vessels allowing injected drugs and fluids to be absorbed quickly into systemic circulation. The hyaluronan rebuilds naturally, and the barrier is completely restored, e.g., within 48 hours.Addition of hyaluronidase in the injectable pharmaceutical formulations increases bioavailability of the MASP-2 inhibitory antibody following parenteral administration, particularly subcutaneous administration. It also allows for greater injection site volumes (i.e., greater than 1 mL) with less pain and discomfort, and minimizes the incidence of injection site reactions (e.g., flattens the injection site bump). In some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody (e.g., OMS646) formulation of the present disclosure comprise from about 100 U / mL to about 20,000 U / mL of a hyaluronidase enzyme. The actual concentration of the hyaluronidase enzyme depends on the type of hyaluronidase enzyme used in the preparation of the MASP-2 inhibitory antibody formulations of the present invention. An effective amount of the hyaluronidase can be determined by the person skilled in the art. It should be provided in sufficient amount so that an increase in the dispersion and absorption of the co-administered or sequentially administered MASP-2 inhibitory antibody is possible. The minimal amount of the hyaluronidase enzyme is greater than 100 U / mL. More particularly, the effective amount of the hyaluronidase enzyme is from about 150U / mL to about 20,000U / mL, whereby the said amount corresponds to about 0.01 mg to 0.16 mg protein based on an assumed specific activity of 100,000 U / mg.In some embodiments, the pharmaceutical formulations comprise hyaluronidase in concentration of about 1,000 to about 20,000 U / ml, such as about 1,000 to about 16,000 U / ml. Alternatively, the concentration of the hyaluronidase is about 1,500 to about 12,000 U / mL, or more particularly about 2,000 U / mL to about 12,000 U / mL. The amounts specified herein correspond to the amount of hyaluronidase initially added to the pharmaceutical formulation. In some embodiments, the ratio (w / w) of the hyaluronidase to the MASP-2 inhibitory antibody is in the range of 1:1,000 to 1:8,000, or in the range of 1:4,000 to 1:6,000 or in the range of about 1:4,000 to 1:5000. The hyaluronidase may be present as a component of the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation of the present disclosure, or it may be provided as a separate solution in a kit-of-parts. Thus, in one embodiment, the MASP-2 inhibitory antibody is co-formulated with a hyaluronidase. In another embodiment, the MASP-2 inhibitory antibody and hyaluronidase are formulated separately and mixed just prior to subcutaneous administration. In yet another embodiment, the MASP-2 inhibitory antibody and hyaluronidase are each formulated and administered separately, e.g., the hyaluronidase is administered as a separate injection directly before or after administration of the formulation comprising the MASP-2 inhibitory antibody.In some instances, the hyaluronidase is administered subcutaneously from about 5 seconds to about 30 minutes prior to the injection of the pharmaceutical formulation comprising the MASP-2 inhibitory antibody of the present disclosure into the same injection site area. In certain embodiments, the pharmaceutical formulation of MASP-2 inhibitory antibody and hyaluronidase solution are included in separate chambers of a pharmaceutical device which automates delivery, either simultaneously (e.g., using a dual barrel syringe) or sequentially. Pre-filled Containers In a further aspect of the present disclosure, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation as disclosed herein is contained in a pre-filled sealed container in an amount sufficient for administration to a mammalian subject. Thus a sufficient quantity of drug composition formulated in accordance with the present disclosure, that is equal or just slightly more (i.e., not more than 25% excess, such as not more than 10% excess) than the amount of MASP-2 inhibitory antibody desired to be administered to a mammalian subject is contained within a pre-filled container that facilitates dispensing the antibody formulation for parenteral administration (i.e., injection or infusion). In some embodiments, the pre-filled container comprises at least one pharmaceutical unit dosage form of the MASP-2 inhibitory antibody. For example, a desired single-use quantity of high-concentration, low-viscosity MASP-2 inhibitory antibody formulation may be packaged in pre-filled container, such as, for example, a glass vial closed with a stopper or other closure that includes a septum through which a hypodermic needle may be inserted to withdraw the formulation, or may be packaged in a pre-filled syringe or other pre-filled container suitable for injection (e.g., subcutaneous injection) or infusion. Examples of such containers include, without limitation, vials, syringes, ampoules, bottles, cartridges, and pouches.Preferably the containers are each single-use prefilled syringes, which may suitably be formed of glass or a polymeric material such as a cyclic olefin polymers or acrylonitrile butadiene styrene (ABS), polycarbonate (PC), polyoxymethylene (POM), polystyrene (PS), polybutylene terephthalate (PBT), polypropylene (PP), polyethylene (PE), polyamide (PA), thermoplastic elastomer (TPE), and their combinations. The barrels of such syringes are operated with an elastomer plunger which can be urged along the barrel to eject liquid content via a needle connected thereto. In some embodiments of the invention, each syringe includes a needle affixed thereto. In some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation as disclosed herein is contained within a pre-filled container selected from the group consisting of: a syringe (e.g., a single or double barreled syringe), a pen injector, a sealed vial (e.g., a dual chamber vial), an auto-injector, a cassette, and a pump device (e.g., an on-body patch pump, a tethered pump or an osmotic pump). For subcutaneous delivery, the formulation may be contained within a pre-filled device suitable for subcutaneous delivery, such as, for example, a pre-filled syringe, autoinjector, injection device (e.g., the INJECT-EASETM, or GENJECTTMdevice), injector pen (such as the GENPENTM) or other device suitable for subcutaneous administration. The formulations of the present disclosure can be prepared as unit dosage forms in a pre-filled container, which can be particularly suitable for self-administration. For example, a unit dosage per vial, cartridge or other pre-filled container (e.g., pre-filled syringe or disposable pen) may contain about 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, 1.1 mL, 1.2 mL, 1.3 mL, 1.4 mL, 1.5 mL, 1.6 mL, 1.7 mL, 1.8 mL, 1.9 mL, 2.0 mL, 2.1 mL, 2.2 mL, 2.3 mL, 2.4 mL, 2.5 mL, 2.6 mL, 2.7 mL, 2.8 mL, 2.9 mL, 3.0 mL, 3.5 mL, 4.0 mL, 4.5 mL, 5.0 mL, 5.5 mL, 6.0 mL, 6.5 mL, 7.0 mL, 7.5 mL, 8.0 mL, 8.5 mL, 9.0 mL, 9.5 mL, or about 10.0 mL or greater volume of the high concentration formulation containing various concentrations of MASP-2 inhibitory antibody (e.g., OMS646) ranging from about 100 mg / mL to about 250 mg / mL, about 150 mg / mL to about 200 mg / mL, about 175 mg / mL to about 200 mg / mL, such as about 185 mg / mL, resulting in a total unit dosage of OMS646 per container ranging from about 20 mg to about 1000 mg or higher. In some embodiments, the formulation of the present disclosure is prepared as a unit dosage form in a pre-filled container, such as a vial or syringe, at a unit dosage of about 350mg to 400mg, such as about 350mg, about 360mg, about 370mg, about 380mg, about 390mg, or about 400mg. In some embodiments, the formulations of the present disclosure are prepared as unit dosage forms in a pre-filled syringe with a volume of from 0.1 mL to 3.0 mL, such as about 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, 1.1 mL, 1.2 mL, 1.3 mL, 1.4 mL, 1.5 mL, 1.6 mL, 1.7 mL, 1.8 mL, 1.9 mL, 2.0 mL, 2.1 mL, 2.2 mL, 2.3 mL, 2.4 mL, 2.5 mL, 2.6 mL, 2.7 mL, 2.8 mL, 2.9 mL, or about 3.0 mL comprising from about 20 mg to 750 mg of the MASP-2 inhibitory antibody (e.g., OMS646). As described herein, the stable formulations prepared as unit dosages can be administered to a subject directly (e.g., via subcutaneous injection), or alternatively are prepared to be suitable for dilution prior to intravenous administration. The formulations of the present disclosure may be sterilized by various sterilization methods suitable for antibody formulations, such as sterile filtration. In certain embodiments the antibody formulation is filter-sterilized, for example, with a presterilized 0.2 micron filter. Sterilized formulations of the present disclosure may be administered to a subject to prevent, treat or ameliorate a disease or disorder associated with MASP-2-dependent complement activation. In a related aspect, the present disclosure provides a method of making an article of manufacture comprising filing a container with a high concentration MASP-2 inhibitory antibody formulation of the present disclosure. In one embodiment, the present disclosure provides a pharmaceutical composition for use in treating a patient suffering from, or at risk for developing a MASP-2-dependent disease or condition, wherein the composition is a sterile, single-use dosage form comprising from about 350 mg to about 400 mg (i.e., 350 mg, 360 mg, 370 mg, 380 mg, 390 mg, or 400 mg) of MASP-2 inhibitory antibody, wherein the composition comprises about 1.8mL to about 2.2 mL (i.e., 1.8 mL, 1.9mL, 2.0 mL, 2.1 mL or 2.2 mL) of a 185 mg / mL antibody formulation, such as disclosed herein, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and (ii) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3; and wherein the formulation is stable when stored at between 2oC and 8oC for at least six months.In some embodiments, the MASP-2 dependent disease or condition is selected from the group consisting of aHUS, HSCT-TMA, IgAN and Lupus Nephritis (LN). Kits comprising high-concentration, low-viscosity MASP-2 inhibitory antibody formulations The present disclose also features therapeutic kits comprising at least one container including the high-concentration, low-viscosity MASP-2 inhibitory antibody formulation as disclosed herein. In some embodiments, the present disclosure provides a kit comprising (i) a container comprising any of the formulations comprising MASP-2 inhibitory antibody described herein; and (ii) a suitable means for delivering the formulation to a patient in need thereof. In some embodiments of any of the kits described herein, the means is suitable for subcutaneous delivery of the formulation to the patient. Various types of containers are suitable for containment of pharmaceutical formulations of MASP-2 inhibitory antibody included in the kits of the present invention. In certain embodiments of the kits of the present invention, the container is a prefilled syringe (e.g., a single barrel or double-barreled syringe) or a prefilled sealed vial. In some embodiments, the container comprising a formulation comprising MASP-2 inhibitory antibody is a pre-filled container selected from the group consisting of: a syringe (e.g., a single or double barreled syringe), a pen injector, a sealed vial (e.g., dual chamber vials), an auto-injector, a cassette, and a pump device (e.g., an on-body patch pump or a tethered pump or an osmotic pump). For subcutaneous delivery, the formulation may be contained within a pre-filled device suitable for subcutaneous delivery, such as, for example, a pre-filled syringe, autoinjector, injection device (e.g., the INJECT-EASETM, and GENJECTTMdevice), injector pen (such as the GENPENTM) or other device suitable for subcutaneous administration. In addition to a container pre-filled with a single-dose of the pharmaceutical formulation, the kit of the present invention may also include an outer container into which such pre-filled container is placed. For example, the outer container may include a plastic or paperboard tray into which recesses are formed that receive the pre-filled container and immobilize it during shipping and handling prior to use. In some embodiments, the outer container is suitably opaque and acts to shield the pre-filled container from light to prevent light induced degradation of the components of the pharmaceutical formulation. For example, the plastic or paperboard tray that receives pre-filled container may be further packaged within a paperboard carton that provides light shielding.The kit of the present invention may also include a set of instructions for administration and use of the MASP-2 inhibitory antibody formulations in accordance with the present invention, which may be printed on the outer container or printed on a sheet of paper that is contained within the outer container. In some embodiments, the kits comprise a second container (e.g., a prefilled syringe) containing an effective dose of a hyaluronidase. The kit may further include other materials desirable from a commercial and user standpoint, including needles, syringes, package inserts and the like. Exemplary Formulations As described above, the stable, high-concentration, low-viscosity MASP-2 inhibitory antibody formulations of the present disclosure include MASP-2 inhibitory antibody a concentration of from 50 mg / mL to 250 mg / mL in an aqueous solution comprising a buffering agent having a pH of 4.0 to 8.0. The buffer system, such as histidine, citrate or succinate, is suitably included at a concentration of from about 10 mM to about 50 mM, and preferably at about 20 mM. In some preferred embodiments, the formulation further comprises an amino acid with a charged side chain at a concentration of from 50 mM to 300 mM. In some embodiments, the formulation comprises an amino acid with a positively charged side chain, such as arginine, at a concentration of from 50 mM to 300 mM. In some preferred embodiments, the formulation further comprises a non-ionic surfactant, such as polysorbate 80, in an amount from 0.001 % (w / v) to 0.1 % (w / v), such as about 0.05% (w / v) to about 0.1% (w / v). In some embodiments, the formulation further comprises a hyaluronidase enzyme in an amount effective to increase the dispersion and / or absorption of the MASP-2 inhibitory antibody following subcutaneous administration. In some embodiments the stable high-concentration, low-viscosity MASP-2 inhibitory antibody formulations of the present disclosure comprise, consist of, or consist essentially of one of the following compositions: a) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM of a histidine buffer at a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine; and optionally 100 to 20,000 U / mL of a hyaluronidase. b) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM of a histidine buffer at a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, about 0.01% to 0.08% (w / v) of a nonionic surfactant; and optionally 100 to 20,000 U / mL of a hyaluronidase. c) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM of a citrate buffer at a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, and optionally 100 to 20,000 U / mL of a hyaluronidase. d) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM of a citrate buffer at a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, about 0.01% to 0.08% (w / v) of a nonionic surfactant; and optionally 100 to 20,000 U / mL of a hyaluronidase. e) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM of a succinate buffer at a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, and optionally 100 to 20,000 U / mL of a hyaluronidase. f) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM of a succinate buffer at a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, about 0.01% to 0.08% (w / v) of a nonionic surfactant; and optionally 100 to 20,000 U / mL of a hyaluronidase. In certain embodiments, the stable high-concentration, low-viscosity MASP-2 inhibitory antibody formulations of the present disclosure comprise, consist of, or consist essentially of one of the following compositions: g) 185 + 18.5 mg / mL MASP-2 inhibitory antibody; 20±2 mM citrate buffer at a pH of about 5.8; 200±20 mM arginine, and optionally 100 to 20,000 U / mL of a hyaluronidase. h) 185 + 18.5 mg / mL MASP-2 inhibitory antibody; 20±2 mM citrate buffer at a pH of about 5.8; 200±20 mM arginine, about 0.01% (w / v) polysorbate 80, and optionally 100 to 20,000 U / mL of a hyaluronidase. i) 185 + 18.5 mg / mL MASP-2 inhibitory antibody; 20±2 mM histidine buffer at a pH of about 5.9, 200±20 mM arginine, and optionally 100 to 20,000 U / mL of a hyaluronidase. j) 185 + 18.5 mg / mL MASP-2 inhibitory antibody; 20±2 mM histidine buffer at a pH of about 5.9, 200±20 mM arginine, about 0.01% polysorbate 80, and optionally 100 to 20,000 U / mL of a hyaluronidase. Methods of producing high-concentration, low-viscosity MASP-2 inhibitory antibody formulations In another aspect, the present disclosure provides a method for producing a formulation comprising 100 mg / mL or greater of a MASP-2 inhibitory antibody, the method comprising: (a) providing a first pharmaceutical formulation comprising purified OMS646, the first pharmaceutical formulation having a first formulation and comprising no more than 50 mg / mL of the OMS646 protein; (b) subjecting the first pharmaceutical formulation to filtration to thereby produce a second pharmaceutical formulation, wherein the second pharmaceutical formulation has a second formulation as a result of the filtration; and (c) concentrating the second pharmaceutical formulation to produce a concentrated antibody solution comprising 100 mg / mL or greater of OMS646. The formulated bulk solution is typically set at a fixed protein concentration so that the desired fill volume can be kept constant.The liquid drug product manufacturing process typically involves mixing the MASP-2 inhibitory antibody with the buffering system, excipients and optionally surfactant, followed by aseptic filtration and filling in vials (or other container, such as syringes) and sealing (e.g., stoppering, capping, or the like). TABLE 1 : Example Formulation 1 Component (USP) added to water for injection Concentration OMS646 antibody 185 mg / mL Sodium Citrate 20 mM L-Arginine HCL 200 mM Polysorbate 80 0.01% TABLE 2 : Example Formulation 2 Component (USP) added to water for injection Concentration OMS646 antibody 185 mg / mL L-Histidine 20 mM L-Arginine HCL 200 mM Polysorbate 80 0.01% Methods of Treatment In another aspect, the present disclosure provides a method of treating a patient suffering from, or at risk for developing a MASP-2-dependent complement-associated disease or disorder comprising administering a high concentration low viscosity formulation comprising a MASP-2 inhibitory antibody (e.g., OMS646) as disclosed herein. As described in U.S. Patent No. 7,919,094; U.S. Patent No. 8,840,893; U.S. Patent No. 8,652,477; U.S. Patent No. 8,951,522, U.S. Patent No. 9,011,860, U.S. Patent No. 9,644,035, U.S. Patent Application Publication Nos. US2013 / 0344073, US2013 / 0266560, US 2015 / 0166675, US2017 / 0137537, US2017 / 0189525 and co-pending U.S. Patent Application Serial Nos. 15 / 476,154, 15 / 347,434, 15 / 470,647, 62 / 315,857, 62 / 275,025 and 62 / 527,926 (each of which is assigned to Omeros Corporation, the assignee of the instant application, each of which is hereby incorporated by reference), MASP-2-dependent complement activation has been implicated as contributing to the pathogenesis of numerous acute and chronic disease states. For example, as described in U.S. Patent No.8,951,522, the primary function of the complement system, a part of the innate immune system, is to protect the host against infectious agents, however, inappropriate or over-activation of the complement system can lead to serious disease, such as thrombotic microangiopathies (TMAs, including aHUS, TTP and HUS) in which endothelial damage as well as fibrin and platelet-rich thrombi in the microvasculature lead to organ damage. The lectin pathway plays a dominant role in activating complement in settings of endothelial cell stress or injury, and preventing the activation of MASP-2 and the lectin pathway halts the sequence of enzymatic reactions that lead to the formation of the membrane attack complex, platelet activation and leukocyte recruitment. As described in U.S. Patent No. 8,652,477, in addition to initiation of the lectin pathway, MASP-2 can also activate the coagulation system and is capable of cleaving prothrombin to thrombin. As described in Example 1 and U.S. Patent No. 9,011,860, OMS646 is a potent inhibitor of lectin-dependent complement activation. This antibody shows no significant binding (at least 5000-fold lower affinity) to the other complement pathway serine proteases C1r, C1s, MASP-1 and MASP-3, and does not inhibit classical pathway dependent complement activation. Accordingly, in some embodiments, the method comprises administering to a patient suffering from or a risk for developing a MASP-2-dependent complement-associated disease or disorder an amount of any of the high-concentration, low-viscosity MASP-2 inhibitory antibody formulations disclosed herein in an amount sufficient to inhibit MASP-2 dependent complement activation in said mammalian subject to thereby treat the disease or disorder. In some embodiments, the methods can be performed using any of the kits or pre-filled containers (e.g., pre-filled syringes or vials) described herein. In some embodiments, the method can further comprise, prior to administering the formulation to the patient, determining that the patient is afflicted with the lectin complement-associated disease or disorder. In some embodiments, the method further comprises administering a tissue permeability modifier (e.g., hyaluronidase) that increases the absorption or dispersion of the MASP-2 inhibitory antibody following parenteral administration. The tissue permeability modifier may be co-administered with the MASP-2 inhibitory antibody formulation or administered sequentially (e.g., within 5 minutes of administering the MASP-2 inhibitory antibody formulation at or near the same injection site). In some embodiments, the method comprises injecting a subject in need thereof from a first prefilled syringe containing a high concentration low viscosity formulation comprising MASP-2 inhibitory antibody (e.g., OMS646) to inhibit MASP-2-dependent complement activation. In some embodiments, the method further comprises injecting the subject from a second pre-filled syringe containing a, wherein the injection is at or near the site of the injection with the MASP-2 inhibitory antibody. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a thrombotic microangiopathy (TMA) including thrombotic thrombocytopenic purpura (TTP), refractory TTP, Upshaw-Schulman Syndrome (USS), hemolytic uremic syndrome (HUS), atypical hemolytic syndrome (aHUS), non-Factor H-dependent atypical hemolytic syndrome, aHUS secondary to an infection, plasma therapy-resistant aHUS, a TMA secondary to cancer, a TMA secondary to chemotherapy, a TMA secondary to transplantation, or a TMA associated with hematopoietic stem cell transplant. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a renal condition including, but not limited to, mesangioproliferative glomerulonephritis, membranous glomerulonephritis, membranoproliferative glomerulonephritis (mesangiocapillary glomerulonephritis), acute post infectious glomerulonephritis (poststreptococcal glomerulonephritis), C3 glomerulopathy, cryoglobulinemic glomerulonephritis, pauci-immune necrotizing crescentic glomerulonephritis, lupus nephritis, Henoch - Schonlein purpura nephritis and IgA nephropathy. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is renal fibrosis (e.g., tubulointerstitial fibrosis) and / or proteinuria in a subject suffering from or at risk for developing chronic kidney disease, chronic renal failure, glomerular disease (e.g., focal segmental glomerulosclerosis), an immune complex disorder (e.g., IgA nephropathy, membranous nephropathy), lupus nephritis, nephrotic syndrome, diabetic nephropathy, tubulointerstitial damage and glomerulonepthritis (e.g., C3 glomerulopathy), or a disease or condition associated with proteinuria, including, but not limited to nephrotic syndrome, pre-eclampsia, eclampsia, toxic lesions of kidneys, amyloidosis, collagen vascular diseases (e.g., systemic lupus erythematosus), dehydration, glomerular diseases (e.g., membranous glomerulonephritis, focal segmental glomerulonephritis, C3 glomerulopathy, minimal change disease, lipoid nephrosis), strenuous exercise, stress, benign orthostatis (postural) proteinuria, focal segmental glomerulosclerosis, IgA nephropathy (i.e., Berger’s disease), IgM nephropathy, membranoproliferative glomerulonephritis, membranous nephropathy, minimal change disease, sarcoidosis, Alport’s syndrome, diabetes mellitus (diabetic nephropathy), drug-induced toxicity (e.g., NSAIDS, nicotine, penicillamine, lithium carbonate, gold and other heavy metals, ACE inhibitors, antibiotics (e.g., adriamycin) or opiates (e.g., heroin) or other nephrotoxins); Fabry’s disease, infections (e.g., HIV, syphilis, hepatitis A, B or C, poststreptococcal infection, urinary schistosomiasis); aminoaciduria, Fanconi syndrome, hypertensive nephrosclerosis, interstitial nephritis, sickle cell disease, hemoglobinuria, multiple myeloma, myoglobinuria, organ rejection (e.g., kidney transplant rejection), ebola hemorrhagic fever, Nail patella syndrome, familial mediterranean fever, HELLP syndrome, systemic lupus erythematosus, Wegener’s granulomatosis, Rheumatoid arthritis, Glycogen storage disease type 1, Goodpasture’s syndrome, Henoch-Schönlein purpura, urinary tract infection which has spread to the kidneys, Sjögren’s syndrome and post-infections glomerulonepthritis. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an inflammatory reaction resulting from tissue or solid organ transplantation including, but not limited to, allotransplantation or xenotransplantation of whole organs ( e.g. , kidney, heart, liver, pancreas, lung, cornea, and the like) or tissue grafts ( e.g. , valves, tendons, bone marrow, and the like). In some embodiments, the MASP-2-dependent complement-associated disorder is an ischemia reperfusion injury (I / R), including but not limited to, myocardial I / R, gastrointestinal I / R, renal I / R, and I / R following an aortic aneurism repair, I / R associated with cardiopulmonary bypass, cerebral I / R, stroke, organ transplant or reattachment of severed or traumatized limbs or digits; revascularization to transplants and / or replants, and hemodynamic resuscitation following shock and / or surgical procedures. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a complication associated with non-obese diabetes (Type-1 diabetes or Insulin-dependent diabetes mellitus) and / or complications associated with Type-1 or Type-2 (adult onset) diabetes including, but not limited to diabetic angiopathy, diabetic neuropathy, diabetic retinopathy or diabetic macular edema. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a cardiovascular disease or disorder, including but not limited to, Henoch - Schonlein purpura nephritis, systemic lupus erythematosus - associated vasculitis, vasculitis associated with rheumatoid arthritis (also called malignant rheumatoid arthritis), immune complex vasculitis, and Takayasu's disease; dilated cardiomyopathy; diabetic angiopathy; Kawasaki's disease (arteritis); venous gas embolus (VGE); and inhibition of restenosis following stent placement, rotational atherectomy and / or percutaneous transluminal coronary angioplasty (PTCA). In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an inflammatory gastrointestinal disorder, including but not limited to, pancreatitis, diverticulitis and bowel disorders including Crohn's disease, ulcerative colitis, irritable bowel syndrome and inflammatory bowel disease (IBD). In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a pulmonary disorder, including but not limited to, acute respiratory distress syndrome, transfusion - related acute lung injury, ischemia / reperfusion acute lung injury, chronic obstructive pulmonary disease, asthma, Wegener's granulomatosis, antiglomerular basement membrane disease (Goodpasture's disease), meconium aspiration syndrome, aspiration pneumonia, bronchiolitis obliterans syndrome, idiopathic pulmonary fibrosis, acute lung injury secondary to burn, non - cardiogenic pulmonary edema, transfusion - related respiratory depression and emphysema. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a extracorporeal exposure - triggered inflammatory reaction and the method comprises treating a subject undergoing an extracorporeal circulation procedure including, but not limited to, hemodialysis, plasmapheresis, leukopheresis, extracorporeal membrane oxygenation (ECMO), heparin - induced extracorporeal membrane oxygenation LDL precipitation (HELP) and cardiopulmonary bypass (CPB). In some embodiments, the MASP-2-dependent complement-associated disease or disorder is inflammatory or non - inflammatory arthritides and other musculoskeletal disorders, including but not limited to, osteoarthritis, rheumatoid arthritis, juvenile rheumatoid arthritis, gout, neuropathic arthropathy, psoriatic arthritis, ankylosing spondylitis or other spondyloarthropathies and crystalline arthropathies, muscular dystrophy and systemic lupus erythematosus (SLE). In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a skin disorder, including, but not limited to, psoriasis, autoimmune bullous dermatoses, eosinophilic spongiosis, bullous pemphigoid, epidermolysis bullosa acquisita, atopic dermatitis, herpes gestationis and other skin disorders, and for the treatment of thermal and chemical burns including capillary leakage caused thereby. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a peripheral nervous system (PNS) and / or central nervous system (CNS) disorder or injury including, but not limited to, multiple sclerosis (MS), myasthenia gravis (MG), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS), Guillain Barre syndrome, reperfusion following stroke, degenerative discs, cerebral trauma, Parkinson's disease (PD), Alzheimer's disease (AD), Miller - Fisher syndrome, cerebral trauma and / or hemorrhage, traumatic brain injury, demyelination and meningitis. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is sepsis or a condition resulting from sepsis including without limitation severe sepsis, septic shock, acute respiratory distress syndrome resulting from sepsis, hemolytic anemia, systemic inflammatory response syndrome, or hemorrhagic shock. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is a urogenital disorder including, but not limited to, painful bladder disease, sensory bladder disease, chronic abacterial cystitis and interstitial cystitis, male and female infertility, placental dysfunction and miscarriage and pre - eclampsia. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an inflammatory reaction in a subject being treated with chemotherapeutics and / or radiation therapy, including without limitation for the treatment of cancerous conditions. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an angiogenesis-dependent cancer, including but not limited to, a solid tumor(s), blood borne tumor(s), high-risk carcinoid tumors and tumor metastases. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an angiogenesis-dependent benign tumor, including but not limited to hemangiomas, acoustic neuromas, neurofibromas, trachomas, carcinoid tumors and pyogenic granulomas. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an endocrine disorder including, but not limited to, Hashimoto's thyroiditis, stress, anxiety and other potential hormonal disorders involving regulated release of prolactin, growth or insulin - like growth factor, and adrenocorticotropin from the pituitary. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an ophthalmic disease or disorder including, but not limited to age - related macular degeneration, glaucoma and endophthalmitis. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is an ocular angiogenic disease or condition including, but not limited to age-related macular degeneration, uveitis, ocular melanoma, corneal neovascularization, primary pterygium, HSV stromal keratitis, HSV-1-induced corneal lymphangiogenesis, proliferative diabetic retinopathy, diabetic macular edema, retinopathy of prematurity, retinal vein occlusion, corneal graft rejection, neovascular glaucoma, vitreous hemorrhage secondary to proliferative diabetic retinopathy, neuromyelitis optica and rubeosis. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is disseminated intravascular coagulation (DIC) or other complement mediated coagulation disorder, including DIC secondary to sepsis, severe trauma, including neurological trauma ( e.g. , acute head injury, see Kumura et al. , Acta Neurochirurgica 85 :23-28 (1987), infection (bacterial, viral, fungal, parasitic), cancer, obstetrical complications, liver disease, severe toxic reaction ( e.g. , snake bite, insect bite, transfusion reaction), shock, heat stroke, transplant rejection, vascular aneurysm, hepatic failure, cancer treatment by chemotherapy or radiation therapy, burn, or accidental radiation exposure. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is selected from the group consisting of acute radiation syndrome, dense deposit disease, Degos Disease, Catastrophic Antiphospholipid Syndrome (CAPS), Behcet’s disease, cryoglobulinemia; paroxysmal nocturnal hemoglobinuria ("PNH") and cold agglutinin disease. In some embodiments, the MASP-2-dependent complement-associated disease or disorder is selected from the group consisting of aHUS, HSCT-TMA, IgAN, and Lupus Nepthritis (LN). Atypical hemolytic uremic syndrome (aHUS) Atypical hemolytic uremic syndrome (aHUS) is part of a group of conditions termed “Thrombotic microangiopathies.” In the atypical form of HUS (aHUS), the disease is associated with defective complement regulation and can be either sporadic or familial. Familial cases of aHUS are associated with mutations in genes coding for complement activation or complement regulatory proteins, including complement factor H, factor I, factor B, membrane cofactor CD46 as well as complement factor H-related protein 1 (CFHR1) and complement factor H-related protein 3 (CFHR3). (Zipfel, P.F., et al., PloS Genetics 3 (3):e41 (2007)). The unifying feature of this diverse array of genetic mutations associated with aHUS is a predisposition to enhanced complement activation on cellular or tissue surfaces. A subject is a risk for developing aHUS upon the onset of at least one or more symptoms indicative of aHUS (e.g., the presence of anemia, thrombocytopenia and / or renal insufficiency) and / or the presence of thrombotic microangiopathy in a biopsy obtained from the subject. The determination of whether a subject is at risk for developing aHUS comprises determining whether the subject has a genetic predisposition to developing aHUS, which may be carried out by assessing genetic information (e.g. from a database containing the genotype of the subject), or performing at least one genetic screening test on the subject to determine the presence or absence of a genetic marker associated with aHUS (i.e., determining the presence or absence of a genetic mutation associated with aHUS in the genes encoding complement factor H (CFH), factor I (CFI), factor B (CFB), membrane cofactor CD46, C3, complement factor H-related protein 1 (CFHR1), or THBD (encoding the anticoagulant protein thrombodulin) or complement factor H-related protein 3 (CFHR3), or complement factor H-related protein 4 (CFHR4)) either via genome sequencing or gene-specific analysis (e.g., PCR analysis), and / or determining whether the subject has a family history of aHUS. Methods of genetic screening for the presence or absence of a genetic mutation associated with aHUS are well established, for example, see Noris M et al. “Atypical Hemolytic-Uremic Syndrome,” 2007 Nov 16 [Updated 2011 Mar 10]. In: Pagon RA, Bird TD, Dolan CR, et al., editors. GeneReviews™, Seattle (WA): University of Washington, Seattle. As described in US2015 / 0166675, in a human ex vivo experimental model of thrombotic microangiopathy (TMA), OMS646 inhibited complement activation and thrombus formation on microvascular endothelial cells exposed to serum samples from aHUS patients in both the acute phase and in remission. As further described in US2017 / 0137537, data obtained in an open-label Phase 2 clinical trial (i.v. administration of 2-4 mg / kg MASP-2 inhibitory antibody OMS646 once per week for 4 consecutive weeks), treatment with OMS646 showed efficacy in patients with aHUS. Platelet counts in all three aHUS patients in the mid- and high-dose cohorts (two in the mid-dose and one in the high-dose cohort) returned to normal, with a statistically significant mean increase from baseline of approximately 68,000 platelets / mL (p=0.0055). Hematopoietic stem cell transplant-associated TMA (HSCT-TMA ) Hematopoietic stem cell transplant-associated TMA (HSCT-TMA) is a life-threatening complication that is triggered by endothelial injury. The kidney is the most commonly affected organ, though HSCT-TMA can be a multi-system disease that also involves the lung, bowel, heart and brain. The occurrence of even mild TMA is associated with long-term renal impairment. Development of post-allogeneic HSCT-associated TMA differs in frequency based on varying diagnostic criteria and conditioning and graft-versus-host disease prophylaxis regimens, with calcineurin inhibitors being the most frequent drugs implicated (Ho VT et al., Biol Blood Marrow Transplant , 11(8):571-5, 2005). As described in US2017 / 0137537, in an Phase 2 clinical trial ( i.v. administration of 4 mg / kg MASP-2 inhibitory antibody OMS646 once per week for 4 to 8 consecutive weeks) , treatment with OMS646 improved TMA markers in patients suffering from HSCT-TMA, including a statistically significant improvement in LDH and haptoglobin levels. The HSCT-TMA patients treated with OMS646 represent some of the most difficult to treat, thereby demonstrating clinical evidence of a therapeutic effect of OMS646 in patients with HSCT-TMA. Immunoglobulin A nephropathy (IgAN ) Immunoglobulin A nephropathy (IgAN) is an autoimmune kidney disease resulting in intrarenal inflammation and kidney injury. IgAN is the most common primary glomerular disease globally. With an annual incidence of approximately 2.5 per 100,000, it is estimated that 1 in 1400 persons in the U.S. will develop IgAN. As many as 40% of patients with IgAN will develop end-stage renal disease (ESRD). Patients typically present with microscopic hematuria with mild to moderate proteinuria and variable levels of renal insufficiency (Wyatt R.J., et al., N Engl J Med 368(25):2402-14, 2013). Clinical markers such as impaired kidney function, sustained hypertension, and heavy proteinuria (over 1 g per day) are associated with poor prognosis (Goto M et al., Nephrol Dial Transplant 24(10):3068-74, 2009; Berthoux F. et al., J Am Soc Nephrol 22(4):752-61, 2011).Proteinuria is the strongest prognostic factor independent of other risk factors in multiple large observational studies and prospective trials (Coppo R. et al., J Nephrol 18(5):503-12, 2005; Reich H. N., et al., J Am Soc Nephrol 18(12):3177-83, 2007). It is estimated that 15-20% of patients reach ESRD within 10 years of disease onset if left untreated (D’Amico G., Am J Kidney Dis 36(2):227-37, 2000). The diagnostic hallmark of IgAN is the predominance of IgA deposits, alone or with IgG, IgM, or both, in the glomerular mesangium. As described in US2017 / 0189525, in a Phase 2 open-label renal trial (i.v. administration of 4 mg / kg MASP-2 inhibitory antibody OMS646 once per week for 12 consecutive weeks), patients with IgA nephropathy that were treated with OMS646 demonstrated a clinically meaningful and statistically significant decrease in urine albumin-to-creatinine ratios (uACRs) throughout the trial and reduction in 24-hour urine protein levels from baseline to the end of treatment. Lupus Nephritis (LN) A main complication of systemic lupus erythematosus (SLE) is nephritis, also known as lupus nephritis, which is classified as a secondary form of glomerulonephritis. Up to 60% of adults with SLE have some form of kidney involvement later in the course of the disease (Koda-Kimble et al., Koda-Kimble and Young’s Applied Therapeutics: the clinical use of drugs, 10thEd, Lippincott Williams & Wilkins: pages 792-9, 2012) with a prevalence of 20-70 per 100,000 people in the US. Lupus nephritis often presents in patients with other symptoms of active SLE, including fatigue, fever, rash, arthritis, serositis, or central nervous system disease (Pisetsky D.S. et al., Med Clin North Am 81(1):113-28, 1997). Some patients have asymptomatic lupus nephritis; however, during regular follow-up, laboratory abnormalities such as elevated serum creatinine levels, low albumin levels, or urinary protein or sediment suggest active lupus nephritis. As described in U.S. Patent Application No. 15 / 470,647, in a Phase 2 open-label renal trial (i.v. administration of 4 mg / kg MASP-2 inhibitory antibody OMS646 once per week for 12 consecutive weeks), 4 out of 5 patients with Lupus Nephritis (LN) that were treated with an anti-MASP-2 antibody demonstrated a clinically meaningful decrease in 24-hour urine protein levels from baseline to the end of treatment. Administration The high concentration low viscosity MASP-2 inhibitory antibody formulations described herein can be administered to a subject in need of treatment using methods known in the art, such as by single or multiple injections or infusions over a period of time in a suitable manner, e.g., injection or infusion by subcutaneous, intravenous, intraperitoneal, intramuscular. As described herein, parenteral formulations can be prepared in dosage unit form for ease of administration and uniformity of dosage. As used herein the term “unit dosage form” refers to physically discrete units suited as unitary dosages for the subject to be treated; each unit containing a predetermined quantity of active compound calculated to produce the desired therapeutic effect in association with the selected pharmaceutical aqueous solution . For the prevention or treatment of disease, the appropriate dosage of the MASP-2 inhibitory antibody will depend on the type of disease to be treated, the severity and course of the disease. The antibody is suitably administered to the patient at one time or over a series of treatments. Depending on the type and severity of the disease, the MASP-2 inhibitory antibody can be administered at a fixed dose, or in a milligram per kilogram (mg / kg) dose. Exemplary dosages of the MASP-2 inhibitory antibody contained in the formulations described herein include, e.g., about 0.05 mg / kg to about 20 mg / kg, such as about 1 mg / kg, 2 mg / kg, 3 mg / kg, 4 mg / kg, 5 mg / kg, 6 mg / kg, 7 mg / kg, 8 mg / kg, 9 mg / kg, 10 mg / kg, 11 mg / kg, 12 mg / kg, 13 mg / kg, 14 mg / kg, 15 mg / kg, 16 mg / kg, 17 mg / kg, 18 mg / kg, 19 mg / kg or 20 mg / kg which can be administered daily, twice weekly, once weekly, bi-weekly, or monthly. Exemplary fixed dosages of the MASP-2 inhibitory antibody, such as the formulations described herein include, e.g., about 10 mg to about 1000 mg, such as about 50 mg to about 750 mg, such as about 100 mg to about 500 mg, such as about 200 mg to about 400 mg, such as about 200 mg, about 225 mg, about 250 mg, about 275 mg, about 300 mg, about 325 mg, about 350 mg, about 375 mg, or about 400 mg which can be administered daily, twice weekly, once weekly, bi-weekly, or monthly. With regard to delivery volume of the formulations, the concentration of the antibody in a formulation used for a therapeutic application is determined based on providing the antibody in a dosage and volume that is tolerated by, and of therapeutic value to, the patient. For a therapeutic antibody formulation to be administered by injection, the antibody concentration will be dependent on the injection volume (usually from 0.5 mL to 3 mL). Antibody based therapies can require several mg / kg of dosing per day, per week, per month, or per several months. Accordingly, if a MASP-2 inhibitory antibody is to be provided at 1mg / kg to 5 mg / kg (e.g., 1mg / kg, 2 mg / kg, 3 mg / kg, 4 mg / kg or 5 mg / kg) of body weight of the patient, and an average patient weighs 75 kg, then 75 mg to 375 mg of the antibody will need to be delivered in a 0.5 mL to 3.0 mL injection volume. Alternatively, the formulation is provided in a concentration suitable for delivery at more than one injection site per treatment. In a preferred embodiment in which the concentration of the OMS646 antibody in the formulation is about 185 mg / mL, for a dosage of 1 mg / kg to 5 mg / kg of body weight of the patient (assuming 75 kg), the formulation would be delivered subcutaneously in about 0.40 mL to about 2.0 mL injection volume. As described herein, the formulations of the present disclosure are suitable for both intravenous (i.v.) dosage and subcutaneous (s.c.) administration. Depending on the type and severity of the disease, the MASP-2 inhibitory antibody can be administered intravenously at a fixed dose, or in a milligram per kilogram (mg / kg) dose. Exemplary dosages of the MASP-2 inhibitory antibody contained in the formulations described herein can be delivered intravenously by diluting an appropriate amount of the high concentration formulation described herein with a pharmaceutically acceptable diluent prior to administration such that the MASP-2 inhibitory antibody is administered to a human subject at a dosage of e.g., about 0.05 mg / kg to about 20 mg / kg, such as about 1 mg / kg, 2 mg / kg, 3 mg / kg, 4 mg / kg, 5 mg / kg, 6 mg / kg, 7 mg / kg, 8 mg / kg, 9 mg / kg, 10 mg / kg, 11 mg / kg, 12 mg / kg, 13 mg / kg, 14 mg / kg, 15 mg / kg, 16 mg / kg, 17 mg / kg, 18 mg / kg, 19 mg / kg or 20 mg / kg which can be administered daily, twice weekly, once weekly, bi-weekly, or monthly. The MASP-2 inhibitory antibody can also be delivered intravenously at a fixed dosage by diluting an appropriate amount of the high concentration formulation described herein with a pharmaceutically acceptable diluent prior to administration such that the MASP-2 inhibitory antibody is administered to a human subject at a dosage of about 10 mg to about 1000 mg, such as about 50 mg to about 750 mg, such as about 100 mg to about 500 mg, such as about 200 mg to about 400 mg, such as about 200 mg, about 225 mg, about 250 mg, about 275 mg, about 300 mg, such as about 300 mg to about 400 mg, such as about 310 mg, about 320 mg, about 325 mg, about 330 mg, about 340 mg, about 350 mg, about 360 mg, about 370 mg, about 375 mg, about 380 mg, about 390 mg or about 400 mg which can be administered daily, twice weekly, once weekly, bi-weekly, or monthly. In some embodiments, the formulation comprising the MASP-2 inhibitory antibody is diluted into a pharmaceutically-acceptable diluent prior to systemic (e.g., intravenous) delivery. Exemplary diluents which can be used include water for injection, 5% dextrose, 0.9% saline, Ringers solution and other pharmaceutically-acceptable diluents suitable for intravenous delivery. While in no way intended to be limiting, exemplary dosages of a MASP-2 inhibitory antibody to be administered intravenously to treat a subject suffering from a MASP-2-dependent complement disease or disorder include, e.g., about 0.05 mg / kg to about 20 mg / kg, such as about 1 mg / kg, 2 mg / kg, 3 mg / kg, 4 mg / kg, 5 mg / kg, 6 mg / kg, 7 mg / kg, 8 mg / kg, 9 mg / kg, 10 mg / kg, 11 mg / kg, 12 mg / kg, 13 mg / kg, 14 mg / kg, 15 mg / kg, 16 mg / kg, 17 mg / kg, 18 mg / kg, 19 mg / kg or 20 mg / kg which can be administered daily, twice weekly, once weekly, bi-weekly, or monthly.Exemplary fixed dosages of the MASP-2 inhibitory antibody to be delivered intravenously to treat a subject suffering from a MASP-2-dependent complement disease or disorder include, e.g., about 10 mg to about 1000 mg, such as about 50 mg to about 750 mg, such as about 100 mg to about 500 mg, such as about 200 mg to about 400 mg, such as about 200 mg, about 225 mg, about 250 mg, about 275 mg, about 300 mg, about 325 mg, about 350 mg, about 375 mg, or about 400 mg which can be administered daily, twice weekly, once weekly, bi-weekly, or monthly. In some embodiments, the formulation is diluted into a pharmaceutically acceptable diluent and administered to a subject in need thereof with an initial i.v. loading dose (e.g., about 300 mg to about 750 mg, such as about 400 mg to about 750 mg, such as about 300 mg to about 500 mg, such as about 300 mg to about 400 mg, such as about 300 mg , about 310 mg, about 320 mg, about 330 mg, about 340 mg, about 350 mg, about 360 mg, about 370 mg, about 380 mg, about 390 mg, or about 400 mg), followed by one or more subcutaneous injections of the formulation with a dosage of 1mg / kg to 5 mg / kg of body weight, or a fixed dosage of about 100 mg to about 400 mg, such as about 100 mg, about 150 mg, about 200 mg, about 250 mg, about 300 mg, about 350 mg, or about 400 mg. For example, an initial i.v. loading dose may be the preferred administration route in particular instances, such as when a patient is in the hospital or in a clinic and suffering from an acute condition (e.g., aHUS) that requires an initial loading dose followed by maintenance dosing with subcutaneous injection of the formulation. Examples The invention is further illustrated in the following examples, which should not be construed as further limiting. All literature citations herein are expressly incorporated by reference. EXAMPLE 1 This Example demonstrates that OMS646, a monoclonal antibody targeting human MASP-2, binds to human MASP-2 with high affinity and blocks the lectin pathway complement activity. Background A fully human monoclonal antibody targeting human MASP-2 (set forth as SEQ ID NO:1), referred to as “OMS646” was generated as described in WO2012 / 151481, which is hereby incorporated herein by reference. The OMS646 monoclonal antibody comprises a heavy chain variable region (VH) set forth as SEQ ID NO:2 and a light chain variable region (VL) set forth as SEQ ID NO:3. OMS646 is comprised of variable regions of human origin fused to human IgG4 heavy chain and lambda light chain constant regions and is secreted as a disulfide-linked glycosylated tetramer consisting of two identical heavy chains (having the amino acid sequence set forth as 4) and two identical lambda light chains (having the amino acid sequence set forth as SEQ ID NO:5). The Asparagine residue (N) at position 295 of the heavy chain (SEQ ID NO:4) is glycosylated and is indicated in bold and underlined text. Heavy Chain Variable Region Presented below is the heavy-chain variable region (VH) sequence for OMS646. The Kabat CDRs (31-35 (H1), 50-65 (H2) and 95-107 (H3)) are bolded; and the Chothia CDRs (26-32 (H1), 52-56 (H2) and 95-101 (H3)) are underlined. OMS646 heavy chain variable region (VH) (SEQ ID NO:2) QVTLKESGPVLVKPTETLTLTCTVS GFSLS RG KMG VSWIRQPPGKALEW LA HIFSS DEKSYRTSL KSRLTISKDTSKNQVVLTMTNMDPVDTAT YYCARIR RGGIDY WGQGTLVTVSS Light Chain Variable Region Presented below is the light-chain variable region (VL) sequence for OMS646. The Kabat CDRs (24-34 (L1); 50-56 (L2) and 89-97 (L3) are underlined. These regions are the same whether numbered by the Kabat or Chothia system. OMS646 light chain variable region (VL) (SEQ ID NO:3) QPVLTQPPSLSVSPGQTASITCS GEKLGDKYAYW YQQKPGQSPVLVMYQ DKQRPSG IPERFSGSNSGNTATLTISGTQAMDEADYYCQ AWDSSTAVF GGGTKLTVL OMS646 heavy chain IgG4 mutated heavy chain full length polypeptide (445 aa) (SEQ ID NO:4 ) QVTLKESGPVLVKPTETLTLTCTVSGFSLSRGKMGVSWIRQPPGKALEWLAHIFSSDEKSYRTSLKSRLTISKDTSKNQVVLTMTNMDPVDTATYYCARIRRGGIDYWGQGTLVTVSSASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPPCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQF N STYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK OMS646 light chain full length polypeptide (212 aa) (SEQ ID NO:5) QPVLTQPPSLSVSPGQTASITCSGEKLGDKYAYWYQQKPGQSPVLVMYQDKQRPSGIPERFSGSNSGNTATLTISGTQAMDEADYYCQAWDSSTAVFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS As described in WO2012 / 151481, OMS646 binds to MASP-2 and selectively inhibits the lectin pathway and does not substantially inhibit the classical pathway (i.e., inhibits the lectin pathway while leaving the classical complement pathway intact) and also exhibits at least one or more of the following characteristics: said antibody binds human MASP-2 with a K D of 10 nM or less, said antibody binds an epitope in the CCP1 domain of MASP-2, said antibody inhibits C3b deposition in an in vitro assay in 1% human serum at an IC 50 of 10 nM or less, said antibody inhibits C3b deposition in 90% human serum with an IC 50 of 30 nM or less, wherein the antibody is an antibody fragment selected from the group consisting of Fv, Fab, Fab', F(ab) 2 and F(ab') 2 , wherein the antibody is a single-chain molecule, wherein said antibody is an IgG2 molecule, wherein said antibody is an IgG1 molecule, wherein said antibody is an IgG4 molecule, wherein the IgG4 molecule comprises a S228P mutation. As described in WO2012 / 151481, OMS646 was determined to avidly bind to human MASP-2 (SEQ ID NO:1) with >5000 fold selectivity when compared to C1s, C1r, MASP-1 or MASP-3. As shown in this example, OMS646 specifically binds to human MASP-2 with high affinity and has the ability to block lectin pathway complement activity. As shown above, OMS646 comprises (a) a heavy-chain variable region comprising (i) CDR-H1 comprising the amino acid sequence from 31-35 of SEQ ID NO:2, ii) CDR-H2 comprising the amino acid sequence from 50-65 of SEQ ID NO:2, and iii) CDR-H3 comprising the amino acid sequence from 95-107 of SEQ ID NO:2; and (b) a light-chain variable region comprising: i) CDR-L1 comprising the amino acid sequence from 24-34 of SEQ ID NO:3, ii) CDR-L2 comprising the amino acid sequence from 50-56 of SEQ ID NO:3, and iii) CDR-L3 comprising the amino acid sequence from 89-97 of SEQ ID NO:3. As further described in WO2012 / 151481, a variant of OMS646, having a heavy chain variable region with at least 95% identity to SEQ ID NO:2 and a light chain variable region with at least 95% identity to SEQ ID NO:3 was demonstrated to have functional activity similar to OMS646. The OMS646 variant described in WO2012 / 151481 comprises a) a heavy chain variable region comprising: SEQ ID NO:2, or a variant thereof comprising an amino acid sequence having at least 95% identity to SEQ ID NO:2, wherein residue 31 is an R, residue 32 is a G, residue 33 is a K, residue 34 is an M, residue 35 is a G, residue 36 is a V, residue 37 is an S, residue 50 is an L, residue 51 is an A , residue 52 is an H, residue 53 is an I, residue 54 is an F, residue 55 is an S, residue 56 is an S, residue 57 is a D, residue 58 is an E, residue 59 is a K, residue 60 is an S, residue 61 is a Y, residue 62 is an R, residue 63 is a T, residue 64 is an S, residue 65 is an L, residue 66 is a K, residue 67 is an S,residue 95 is a Y, residue 96 is a Y, residue 97 is a C, residue 98 is an A, residue 99 is an R, residue 100 is an I, residue 101 is an R, residue 102 is an R or A, residue 103 is a G, residue 104 is a G, residue 105 is an I, residue 106 is a D and residue 107 is a Y; and b) a light chain variable region comprising: SEQ ID NO:3 or a variant thereof comprising an amino acid sequence having at least 95% identity to SEQ ID NO:3, wherein residue 23 is an S, residue 24 is a G, residue 25 is an E or D, residue 26 is a K, residue 27 is an L, residue 28 is a G, residue 29 is a D, residue 30 is a K, residue 31 is a Y or F, residue 32 is an A, residue 33 is a Y, residue 49 is a Q, residue 50 is a D, residue 51 is a K or N, residue 52 is a Q or K, residue 53 is an R, residue 54 is a P, residue 55 is an S, residue 56 is a G, residue 88 is a Q, residue 89 is an A, residue 90 is a W, residue 91 is a D, residue 92 is an S, residue 93 is an S, residue 94 is a T, residue 95 is an A,residue 96 is a V and residue 97 is an F., 1. OMS646 specifically blocks lectin-dependent activation of terminal complement components Methods: The effect of OMS646 on membrane attack complex (MAC) deposition was analyzed using pathway-specific conditions for the lectin pathway, the classical pathway and the alternative pathway. For this purpose, the Wieslab Comp300 complement screening kit (Wieslab, Lund, Sweden) was used following the manufacturer’s instructions. Results : FIGURE 1A graphically illustrates the amount of lectin pathway-dependent MAC deposition in the presence of different amounts of human MASP-2 inhibitory antibody (OMS646). FIGURE 1B graphically illustrates the amount of classical pathway-dependent MAC deposition in the presence of human MASP-2 inhibitory antibody (OMS646). FIGURE 1C graphically illustrates the amount of alternative pathway-dependent MAC deposition in the presence of different amounts of human MASP-2 inhibitory antibody (OMS646). As shown in FIGURE 1A, OMS646 blocks lectin pathway-mediated activation of MAC deposition with an IC50value of approximately 1 nM. However, OMS646 had no effect on MAC deposition generated from classical pathway-mediated activation (FIGURE 1B) or from alternative pathway-mediated activation (FIGURE 1C). EXAMPLE 2 OMS646 Pre-Formulation Studies Background / Rationale : The composition of a reduced viscosity protein formulation is determined by consideration of several factors including, but not limited to: the nature of the protein, the concentration of the protein, the desired pH range, the temperature at which the protein formulation is to be stored, the period of time over which the protein formulation is to be stored, and how the formulation is to be administered to a patient. For a reduced viscosity formulation to be administered by injection, the protein concentration is dependent upon the injection volume (usually 1.0 mL to 2.25 mL). If a protein is to be provided at 2 to 4 mg / kg of body weight of a patient, and an average patient weighs 75 kg, then 150 mg-300 mg of the protein will need to be delivered in a 1.0 mL to 1.62 mL injection volume. Viscosity is ideally maintained below about 25 cP to ensure a realistically syringeable subcutaneous therapeutic product.In some embodiments, viscosity is maintained below about 20 cP to allow for delivery of the therapeutic product with an injection device, and also to allow for various types of bioprocessing, such as tangential flow filtration. The primary aim of these studies was to identify formulation components that would result in optimal chemical, physical, and structural stability of OMS646 antibody in liquid formulation resulting in a stable formulation with a viscosity of less than 25 cP, such as less than 20 cP, with a high concentration of OMS646 (100 mg / mL or greater) suitable for subcutaneous injection into a human subject. Analytic Methods: To test various buffer and excipient combinations, a purified preparation of OMS646 antibody (102 mg / mL in 20 mM sodium acetate, 50 mg / mL sorbitol, pH 5.0) was diluted to ~ 1 mg / mL in the selected formulation solutions and 4 mL volumes were placed in concentrators pre-rinsed with the appropriate buffer. Each unit was spun down to ~ 1 mL at 3200 x g. This process was repeated for a total of three rounds of buffer-exchange. Formulation appearance was evaluated using an Eisai Machinery Observation Lamp, Model MIH-DX against water using white and black backgrounds. Each formulation sample was tested for color, clarity (opalescence), and the presence of particulate matter. The protein content of OMS646 formulations was determined using an extinction coefficient of 1.49 mL / mg*cm. Measurement of absorbance at 280 nm with correction for absorbance at 320 nm was performed using disposable UVettes and a path length of 0.2 cm. Samples were prepared in duplicate by dilution with 1x Dulbecco’s Phosphate-Buffered Saline (DPBS) to a final concentration of ~2 mg / mL. For high concentration samples, the neat solutions were first diluted 1:1 in formulation buffer, and then diluted to ~2 mg / mL in 1x DPBS. Duplicate measurements for each sample were averaged, and the percent relative standard deviation (RSD) was calculated. For any duplicate samples displaying > 5% RSD, an additional dilution set was prepared and measured. The protein concentration was calculated as follows: Corrected A280 = A280 – A320 Protein Concentration (mg / mL) = (Corrected A280 * Dilution Factor) / 1.49 mL / mg*cm To assess sample turbidity / light scattering, 100 μL of undiluted sample was measured at 320 nm in a disposable UVette using a 1 cm path length. For each sample, the spectrophotometer was blanked with the appropriate buffer-exchange solution without the protein present. Following measurement, samples were recovered and used for pH analysis. In order to normalize turbidity measurements for sample concentration, A320 was also divided by the concentration in mg / mL and the resulting value in mAU*mL / mg was reported. pH measurements of all formulations and solutions were performed at room temperature using a calibrated SevenMulti Meter (Mettler Toledo) with an automatic temperature compensation electrode. The thermal stability of the OMS646 formulations was monitored by differential scanning calorimetry (DSC). Melting temperature (Tm) data for the mAb were collected using a MicroCal Capillary DSC. The protein samples were diluted to a final concentration of ~2 mg / ml in the appropriate buffer-exchange solution. Evaluation of the samples by DSC was performed by scanning from 20-110˚C at 1°C / minute or 2°C / minute. The pre-scan thermostat was set to 10 minutes, post-scan thermostat to 0 minutes, and the post-cycle thermostat set to 25°C. For Tmdata analysis, a buffer-buffer scan was subtracted from the buffer-sample scan and the thermogram was then normalized to protein concentration (molar) using a molecular weight estimate of 150 kDa. A progressive baseline was generated and subtracted from the data to facilitate Tm determination. Melting temperatures were determined using the pick peaks function of the associated Origin® scientific software. Dynamic light scattering (DLS) measures time-dependent fluctuations in the intensity of scattered light from particles in a sample, where the Stokes Einstein equation is used to calculate the hydrodynamic radius of the particle(s) in solution. The DLS experiments for OMS646 formulations were performed with duplicate undiluted samples (30 - 40 μL) using a DynaPro™ Plate Reader II instrument (Wyatt). A total of 10 individual scans were performed at 25°C, with an acquisition time of 5 seconds. Viscosity was set to that of phosphate buffered saline, 1.019 cP. The resultant intensity distribution plots were compared to evaluate the effects of various formulation components on mean particle size by intensity (overall diameter), a global size distribution width parameter (overall percent polydispersity, or % Pd), the average peak diameter of the OMS646 monomer (Peak 2 diameter), and that peak’s width parameter (Peak 2 % Pd).Percent polydispersity (overall or Peak 2) is a width parameter that reflects the heterogeneity detected in the intensity distribution plot, where % Pd < 20% is indicative of a near monodisperse solution and / or species conformation. Stability against chemical denaturation was evaluated using the AVIA Isothermal Chemical Denaturation System (Model 2304), which tests chemical stability under ambient conditions in an automated fashion by generating a denaturant gradient by mixing constant volumes of formulated protein with formulation buffer and formulation buffer containing urea. Briefly, formulated protein was diluted to 0.33 mg / mL in formulation buffer. For a given formulation, a second formulation buffer containing 10M urea was also prepared. Due to solubility issues, 9M urea solutions were prepared for sucrose- and sorbitol-containing formulations. After a uniform incubation time (~30 minutes), intrinsic protein fluorescence (i.e., tryptophan fluorescence) is measured for each data point, where chemical unfolding of the protein results in exposure of buried tryptophans to solvent with an associated red-shift in the fluorescence signal.For each formulation, data was obtained for a total of 24 urea concentrations (0-9.0M for 10 M urea stocks and 0-8.1M for 9M urea stocks), and the ratio of Abs350 / Abs330 was used for baseline subtraction of background fluorescence changes, and a non-linear least squares fit to the unfolding transition data was employed using either a 2-state or 3-state model. Viscosity of the formulations was determined using either a rolling ball viscometer or a rheometer. All viscosity measurements were performed at 25°C with a shear rate in the range of 0.5 s-1to 1000 s-1. Rolling ball measurements were performed using an Anton Paar AMVn viscometer. For rolling ball viscosity measurements, the time a gold ball takes to pass a distance in a capillary filled with the sample is measured after tilting the capillary to a predefined angle (80 degrees). Capillaries were tilted a total of three times and the results were averaged to determine the final dynamic viscosity, a value which is not dependent on sample density. For rolling ball measurements, the capillary was first cleaned using DI water and methanol. Calibration of the instrument / capillary was confirmed by measurement of 10 cP, 50cP and / or 100 cP Brookfield viscosity standards. The capillary was re-cleaned with DI water and methanol prior to and between every sample measurement. Rheometer-based viscosity measurements were performed using a DV-III Ultra Programmable Rheometer which was calibrated with Brookfield Viscosity Standard Fluid #10 and #50. 0.5 mL of each sample was measured at various spindle speeds (shear rates). Samples displaying viscosity (cP) readings with <10% RSD for all shear rates were considered Newtonian over this range, while samples were shear rate-dependent viscosity were considered non-Newtonian. Density measurements were carried out using an Anton Paar DMA 4500M Densitometer. Briefly, the instrument was flushed with DI water several times followed by methanol. The instrument was calibrated for air and water prior to measuring the density of water as a sample. The instrument was again washed with water and methanol and a single sample measurement was performed on ~175 mg / mL material pooled from several formulations. The reported value was used as a reasonable density approximation for high-concentration OMS646 formulations to be used in gravimetric content measurements. Osmolality measurements were performed using a freezing point depression osmometer (Multi-Osmette Osmometer, Precision Systems model 2430), which measures the decrease in a solution’s freezing point as solute concentration increases. A liquid particle-counting system (Hach Model 9703, Sensor Model: HRLD-150) was used for determining particle size and abundance in OMS646 formulation samples. Sample data was obtained using a single 500 µL draw of sample (200 µL tare volume). Briefly, the instrument was allowed to warm up for ~30 minutes and both the syringe (1 mL) and system were flushed with deionized water for at least 10 cycles before use. Environment suitability was tested by showing that 25 mL of deionized water contained no more than 25 particles ≥10 µm in size. System suitability was confirmed by analyzing a single 500 µL draw of 2, 5, 10 and 15 µM standards using appropriate channel sizes. If cumulative counts / mL detected fell within the specification given for the standard, then the system was deemed suitable for sample testing. Before the first sample measurement, the system was flushed once with 1x Phosphate Buffered Saline (PBS) to ensure that samples did not precipitate upon contact with deionized water.Samples were analyzed using a single 500 µL draw, and cumulative counts / mL for 2 µm, 5 µm, 10 µm and 25 µm channels were determined to the nearest whole number. Size exclusion chromatography (SEC) was used to evaluate the quantity of aggregates and degradation products present in the OMS646 formulations. Briefly, an Agilent 1100 HPLC system was fitted with a G3000SWxl SEC column (Tosoh, 7.8 x 300 mm, 5 µm particle size). OMS646 formulation samples were diluted to 2.5 mg / mL in SEC mobile phase (140 mM potassium phosphate, 75 mM potassium chloride, pH 7.0) and 20 µL of sample was injected into the HPLC column. The system was run using a flow rate of 0.4 mL / min, and eluted protein was detected by absorption at 280 nm (bandwidth 4 nm) with no reference correction. To assess system suitability, all samples were bracketed by mobile phase blank and gel filtration standard injections, and reference material was injected in duplicate at the beginning of the sequence.Percent abundances for individual and total high molecular weight (HMW) species and low molecular weight (LMW) species, in addition to percent monomer and total integrated peak area were determined. Analysis by reduced SDS capillary gel (SDS-CE) electrophoresis was performed with a Beckman Coulter PA 800 Plus capillary electrophoresis system and PDA detection module, using an SDS-MW Analysis Kit. Samples and reference were first diluted to 1.0 mg / mL in SDS-MW Sample Buffer. To 95 μL of this working solution 5 μL of β-mercaptoethanol and 2 μL of Internal Standard (10 kDa) were added. All samples were centrifuged at 300 x g for 1 minute, heated at 70 ± 2°C for ~10 minutes, and transferred to a PCR vial and kept at 25°C until analysis. Separations were conducted by applying 15 kV (reverse polarity) across the capillary for 30 minutes and applying a 20.0 psi pressure at both inlet and outlet. Data was acquired at 220 nm with a collection rate of 4 Hz. Reference (unprocessed OMS646) was injected twice at the beginning of each sequence. Percent LC, HC and IgG were reported. Non-reduced SDS capillary gel electrophoresis analyses were carried out as described for reduced CE-SDS, with the exception that freshly prepared 250 mM iodoacetamide was used in place of reducing agent, and separations were performed for 35 minutes. Total electropherogram area and % IgG were reported. A purified preparation of OMS646 antibody (102 mg / mL) was generated using recombinant methods as described in WO2012 / 151481, which is hereby incorporated herein by reference. Briefly described, OMS646 antibody was generated in CHO cells containing expression constructs encoding the heavy chain and light chain polypeptides of OMS646 and purified using standard techniques. 1. Comparison of Candidate Buffering Systems: Methods: In the pre-formulation studies, the stability of MASP-2 inhibitory antibody OMS646 was initially evaluated against a panel of candidate buffers including those commonly used in therapeutic antibody formulation (citrate, histidine, phosphate), as well as more unconventional buffers (acetate, succinate) in order to cover a wide pH range (pH 4.0 – pH 8.0). For this study, the protein was exchanged into 20 mM succinate (pH 4.0, 5.0 and 5.5), acetate (pH 4.0, 5.0 and 5.5), citrate (pH 5.0, 6.0 and 7.0), histidine (pH 6.0 and 7.0) and phosphate (pH 6.0, 7.0 and 8.0) buffers using Amicon Ultra-4 (10 kDa MWCO) concentrators. A purified preparation of OMS646 antibody (102 mg / mL in 20 mM sodium acetate, 50 mg / mL sorbitol, pH 5.0) was diluted to ~1 mg / mL in each of the 14 formulation solutions, and 4.0 mL volumes were placed in concentrators pre-rinsed with the appropriate buffer. Each unit was spun down to ~1 mL at 3200 x g.This process was repeated for a total of three rounds of buffer-exchange. During the final round of concentration, the protein was over-concentrated to < 1 mL. The approximate volume and centrifuge time of each solution was recorded after each cycle. Results : Overall, the data generated for the five buffer types were comparable with regard to buffer-exchange rate, protein content recovery, differential scanning colorimetry (DSC), dynamic light scattering (DLS) and chemical stability (data not shown). Acetate, citrate and histidine were selected for further evaluation based on the apparent overall optimal thermal and conformational OMS646 properties in the pH range 5.5-6.0. Acetate was selected over succinate at pH 5.5 due primarily to superior thermal stability, while histidine and citrate were selected over phosphate at pH 6.0 based upon DLS data. 2. Excipient Screening The stability of OMS646 was evaluated in the presence of various excipients with reported antibody-stabilizing properties, using buffering systems identified during baseline buffer screening (20 mM acetate, pH 5.5; citrate, pH 6.0, and histidine, pH 6.0). For this study, OMS646 was buffer-exchanged into each candidate buffer containing either 150 mM NaCl, 250 mM sorbitol, 250 mM sucrose, 150 mM L-arginine, 150 mM L-glutamate or 250 mM L-proline using Amicon Ultra-4 (10 kDa MWCO) concentrators. Sample preparation was carried out as described in the buffer system comparison wherein the target protein concentration was 2.0 mg / mL. Results : With regard to protein recoveries, the estimated protein recoveries ranged from ~72-106%, which represented a modest improvement over recoveries in the absence of excipient. Histidine buffer appeared to be preferred for the majority of excipients, and acetate and citrate showed mixed results. With regard to DSC, it was observed that citrate buffer resulted in OMS646 thermal stabilization for all excipients tested. FIGURE 2A graphically illustrates the results for Dynamic Light Scattering (DLS) analysis for OMS646 formulation excipient screening, showing the overall particle diameter observed for formulations containing various candidate excipients. FIGURE 2B graphically illustrates the results for DLS analysis for OMS646 formulation excipient screening, showing the overall polydispersity observed for formulations containing various candidate excipients. As shown in FIGURE 2A and 2B, with regard to DLS, most formulations yielded comparable results. However, for all buffering systems, sucrose was associated with elevated polydispersity and the largest overall and monomeric diameters. Following sucrose, sorbitol was the least preferred by DLS, showing larger mean sizes and increased polydispersity.The remaining formulations were generally comparable by DLS with monomer diameters of 10-12 nm (see FIGURE 2A) and polydispersity <20% indicating monodisperse populations (see FIGURE 2B). With regard to stability against chemical denaturation, as evaluated using the AVIA Isothermal Chemical Denaturation System, a buffer / pH trend was clearly observed where acetate pH 5.5 formulations denatured at urea concentrations ~0.5 M lower than citrate and histidine pH 6.0 formulations for all excipients tested. Citrate and histidine were comparable for all excipients. In summary, the data supported citrate at approximately a pH of 6.0 as the optimal buffer / pH combination, which was carried forward into solubility screening studies. Given the poor DLS data observed with all buffer types, sucrose was excluded from further consideration. 3. Solubility / Viscosity Screening First Viscosity Study: Methods: In order to establish conditions for maximum OMS646 solubility, 20 mM citrate (pH 5.0 and 6.0) and 20 mM succinate (pH 4.0) were used in the presence of several isotonic combinations of NaCl, sorbitol, arginine, glutamate and proline. OMS646 was buffer-exchanged using Amicon 15 concentrator units in multiple cycles and on the final cycle the volume of each solution was reduced to ~1 mL. Buffer exchange rates for all formulations and exchange cycles were recorded and analyzed. Following buffer exchange, protein contents were measured, percent recovery was calculated and the samples were stored overnight at 5ºC. During storage, the succinate / glutamate formulation was observed to precipitate and was not evaluated further.Remaining formulations were added to Amicon 4 concentrator units and concentrated until a target concentration of ~200 mg / mL was reached, or until centrifugation no longer resulted in volume reduction and / or sample viscosity (via sample manipulation) was deemed to be unmanageable. Results : With regard to buffer-exchange rates, the highest exchange rates were clearly observed in pH 4.0 samples, with succinate / sorbitol showing the fastest exchange rates overall. Exchange rates at pH 5.0 and 6.0 were comparable, where formations containing only charged amino acid excipients showed higher rates than other formulations. The slowest exchange rate was observed for the citrate / sorbitol formulation at pH 6.0. This formulation was the lone sample with pH ≥ 5.0 and an uncharged excipient component. Under the assumption that exchange rate is a surrogate indicator for OMS646 self-association, it appears that charged species are important for mitigating this behavior at a more neutral pH. With regard to DLS, all high-concentration formulations showed comparable overall diameters of ~12nm, with the exception of succinate / arginine pH 4.0 which showed an elevated global size distribution at >18 nM. The buffer-exchanged samples were concentrated until solutions became physically unworkable due to high viscosity. Maximum concentrations in excess of 225 mg / mL were achieved for both pH 4.0 formulations. For formulations at higher pH values, maximal OMS646 protein concentrations ranged from 160.5 to 207.6 mg / mL. Viscosity for the majority of formulations was evaluated using a rolling ball viscometer with a shear rate between 0.5 s-1to 1000 s-1as described above. FIGURE 3 graphically illustrates the results of viscosity analysis for OMS646 solubility screening over a range of protein concentrations in various formulations as measured at pH 5.0 and pH 6.0. As shown in FIGURE 3, when plotted against protein concentration, an exponential increase in viscosity was observed over the formulations, with the highest viscosity recorded for citrate / arginine / glutamate pH 5.0 (161.1 cP for a 196.6 mg / mL solution). At pH 6.0 and a comparable OMS646 protein concentration, the citrate / sorbitol formulation showed considerably higher viscosity than either the sorbitol / glutamate or proline / glutamate formulation. The citrate / arginine / glutamate pH 6.0 formulation (95.3 mg / mL) displayed approximately half the viscosity (5.8 vs. 9.3 cP) of the citrate / NaCl pH 6.0 sample (87.5 mg / mL) at a higher protein content suggesting an importance of charged amino acids over ionic excipients. It is important to note that at a given concentration (i.e., 125 mg / mL), viscosity varies dramatically as a function of the formulation. Viscosity is ideally maintained below ~25 cP to ensure a realistically syringeable subcutaneous therapeutic product. In some embodiments of the OMS646 formulation, viscosity is maintained below about 20 cP to allow for delivery of the therapeutic product with an injection device, and also to allow for various types of bioprocessing, such as tangential flow filtration. Second Viscosity Study In an effort to reduce OMS646 formulation viscosity and, thus, maximize OMS646 concentration in a given formulation, an additional study was performed. Based on the initial results, the formulations most likely to produce a reduced viscosity formulation at high concentration were selected, namely: succinate / sorbitol pH 4.0 and glutamate-and arginine-containing citrate formulations at pH 6.0. Based on previous studies, charged amino acids were associated with several beneficial properties at neutral pH including increased buffer-exchange rate, increased sample processing recovery, and reduced viscosity. The impact of amino acids with a positively charged side chain (e.g., arginine) or amino acids with a negatively charged side chain (e.g., glutamate) were evaluated over a range of concentrations (50 mM to 150 mM) to gauge both excipient charge and concentration on viscosity.Finally, CaCl2was used as an additive in both isotonic and hypertonic citrate / glutamate solutions due to its potential viscosity reducing properties as described in U.S. Patent No. 7,390,786. Samples were buffer-exchanged and concentrated as described above. Following buffer-exchange, the protein content of all formulations was calculated. The exception was the formulation containing 50 mM glutamate and 50 mM CaCl2, which precipitated following buffer-exchange and was not evaluated further. This is likely due in part to the limited solubility of citrate and divalent cations such as Ca2+. Results : FIGURE 4 graphically illustrates the percent protein recovery following buffer-exchange for the OMS646 solubility / viscosity study with various candidate formulations. As shown in FIGURE 4, a trend towards increasing recovery with increasing arginine concentration was observed, where the 150 mM arginine formulation showed the highest protein recovery at 85%. Recoveries for the remaining formulations were comparable and ranged from 64-75%. Samples were then concentrated as described above until they became manually unworkable. All formulations were evaluated for viscosity as described above and the results are shown below in TABLE 3. TABLE 3 : Summary of the viscosity data from the pre-formulation studies Sample Buffer Excipient Additive pH Conc (mg / mL) Viscosity (cP) 100 cP Standard (97.2 cP Claim) - 97.1 50 cP Standard (49.2 Claim) - 49.1 S1 20 mM Succinate 250 mM sorbitol - 4.0 209.3 109.6 S2 20 mM Citrate 150 mM Arginine - 6.0 181.2 70.5 S3 20 mM Citrate 100 mM Arginine - 6.0 170.8 102.8 S4 20 mM Citrate 50 mM Arginine - 6.0 158.3 140.1 S5 20 mM Citrate 150mM Glutamate - 6.0 180.3 71.2 S6 20 mM Citrate 100 mM Glutamate - 6.0 170.7 74.6 S7 20 mM Citrate 50 mM Glutamate - 6.0 152.7 137.0 S8 20 mM Citrate 150 mM Glutamate 50 mM CaCl 2 6.0 202.8 73.4 As shown above in TABLE 3, viscosities for all formulations were >70 cP, and despite the broad range of final concentrations, clear trends were observed. From this preliminary data, it was evident that increased arginine or glutamate concentration led to reduced viscosity. The viscosity of the succinate / sorbitol formulation appeared comparable to the 150 mM amino acid formulations. Inclusion of CaCl2showed a reduction in viscosity, where viscosity for this formulation was comparable to samples of 10% lower protein content. Four formulations (S1, S2, S5 and S8 shown in TABLE 3) were selected for a more detailed viscosity analysis, where recovered neat samples were incrementally diluted in formulation buffer of 25 mg / mL. FIGURE 5 graphically illustrates the viscosity (as determined by exponential fit of the viscosity data) versus protein concentration for the OMS646 solubility / viscosity study with various candidate formulations. The exponential fit of the viscosity data was determined in accordance with the methods described in Connolly B. et al., Biophysical Journal vol 103:69-78, 2012. As shown in FIGURE 5, the 150 mM glutamate and arginine formulations showed almost identical curves that displayed the highest viscosity per unit concentration- a viscosity of 25 cP equating to ~ 150 mg / mL OMS646. The succinate sorbitol formulation performed somewhat better, with 25 cP corresponding to an estimated OMS646 content of ~160 mg / mL.The lowest overall viscosity was observed in the CaCl2-containing formulation where the estimated content at 25 cP was ~175 mg / mL. The most intriguing result of this analysis was that the hypertonic formulation including 150 mM glutamate and 50 mM CaCl2dramatically reduced sample viscosity. Given the desire for the highest concentration liquid formulation possible, the application of divalent cations and hypertonicity towards viscosity reduction was carried forward into an additional viscosity study. Third Viscosity Study Based on the results from the initial viscosity studies described above, an additional study was carried out to determine whether the apparent viscosity reducing properties of CaCl2were related to the divalent Ca2+or hypertonicity. A change in predominate excipient from glutamate to arginine was performed due to the improved buffer-exchange rates observed for arginine-containing formations. The incorporation of histidine was performed due to the potential for chelation of Ca2+by citrate which could lead to precipitation. A subset of samples also evaluated the impact of pH and surfactant on sample viscosity, as well as the impact of CaCl2and hypertonicity on the succinate / sorbitol pH 4.0 formulation. Samples were buffer-exchanged and concentrated as described for the previous viscosity studies. Viscosity for all formulations was measured using a rolling ball instrument as described above. Viscosity data was normalized to a sample protein concentration of 170 mg / mL.This was performed by first calculating a theoretical viscosity from the measured protein content using the exponential regression to previously calculated Viscosity / Solubility viscosity data from the citrate / arginine pH 6.0 formulation (y=0.0917e0.0361x). The normalized viscosity was calculated by multiplying the theoretical viscosity for citrate / arginine pH 6.0 at 170 mg / mL (42.4 cP) by measured viscosity / theoretical viscosity (see Table 4, footnote b). The resulting normalized viscosities reveal much clearer trends by smoothing concentration-associated variability (see TABLE 4 and FIGURE 6). TABLE 4 . Summary of Viscosity Data for OMS646 (170 mg / mL) formulations Form # Buffer / pH Excipient Additive PS-80 Viscosity (cP) Means Norm Conc (mg / mL) Theor Viscosity (cP) a Approx Norm Viscosity at 170 mg / mL (cP) b 100 cP Standard (97.2 cP Claim) 96.9 - 1A 20 mM Citrate pH 6.0 112.5 mM Arginine 25 mM CaCl 2 - 38.8 165.5 36.0 45.7 1B 112.5 mM Arginine 25 mM CaCl 2 0.05% 41.7 168.5 40.2 44.0 2 150 mM Arginine - - 20.8 155.7 25.3 34.9 3 150 mM Arginine 25 mM CaCl 2 - 20.1 157.0 26.5 32.2 4 200 mM Arginine - - 22.3 169.1 41.0 23.1 5 225 mM Arginine - - 20.2 169.0 40.9 20.9 6A 20 mM Citrate pH 5.0 112.5 mM Arginine 25 mM CaCl 2 - 34.1 165.4 35.9 40.4 6B 112.5 mM Arginine 25 mM CaCl 2 0.05% 31.0 170.0 42.4 31.1 7 150 mM Arginine - - 22.1 158.9 28.4 33.0 8 150 mM Arginine 25 mM CaCl 2 - 17.4 153.9 23.7 31.1 9 20 mM Histidine pH 6.0 75 mM Arginine 50 mM CaCl 2 - 19.9 174.5 49.9 16.9 10A 112.5 mM Arginine 25 mM CaCl 2 - 27.9 169.6 41.8 28.4 10B 112.5 mM Arginine 25 mM CaCl 2 0.05% 28.1 184.6 71.8 16.6 11 135 mM Arginine 10 mM CaCl 2 - 34.1 167.1 38.2 37.9 12 150 mM Arginine - - 35.5 156.6 26.1 57.7 13 200 mM Arginine - - 20.2 167.2 38.3 22.3 14 225 mM Arginine - - 16.4 161.9 31.6 22.0 15 150 mM Arginine 50 mM CaCl 2 - 15.9 164.9 35.2 19.1 16A 20 mM Succinate pH 4.0 125 mM Sorbitol 50 mM CaCl 2 - 19.5 172.7 46.7 17.7 16B 125 mM Sorbitol 50 mM CaCl 2 0.05% 18.1 168.7 40.4 19.0 17 250 mM Sorbitol 50 mM CaCl 2 - 15.5 157.2 26.8 24.6 18 250 mM Sorbitol - 16.8 161.3 31.0 23.0. aTheoretical viscosity was calculated using the regression to the measured content citrate / arginine pH 6.0 viscosity curve ( y=0.0917e0.0361x) bTheoretical viscosity of 170 mg / mL citrate / arginine pH 6.0 (42.4 cP)* (Measured Viscosity / Theor Viscosity) FIGURE 6 graphically illustrates the concentration-normalized viscosity data for the viscosity study with various candidate OMS646 formulations based on the data from TABLE 4. As shown in FIGURE 6 and TABLE 4, for citrate and histidine formulations, examination of the normalized data set clearly shows that hypertonicity leads to reduced sample viscosity, wherein the majority of the impact is observed with only modest increases in arginine concentration. For example, the normalized viscosity of formulation 12 (20 mM histidine with 150 mM arginine) is 57.7 cP, compared with viscosities of 22.3 and 22.0 cP for histidine formulations containing 200 and 225 mM arginine, respectively. A similar trend was observed for citrate / arginine formulations. There was no obvious benefit of CaCl2inclusion. Rather, it was surprising to find that in the absence of CaCl2, low viscosities (e.g., less than 25 cP) were achieved with the citrate / arginine and the histidine / arginine formulations with an arginine concentration of 200 mM or greater. Inclusion of 0.05% PS-80 resulted in substantial viscosity reduction in two of the three formulations evaluated at pH ≥ 5.0. Finally, viscosities at pH 5.0 appeared somewhat lower than those for comparable formulations at pH 6.0. In view of the results obtained from the viscosity studies, hypertonic arginine, the presence or absence of divalent cations and the succinate / sorbitol pH 4.0 formulations were carried forward into surfactant screening studies to further evaluate the impact on OMS646 physical, conformation, and chemical stability. 4. Surfactant Screening The impact of surfactant on OMS646 stability was evaluated using candidate formulations identified in prior studies described herein. For surfactant screening studies, six formulations were analyzed as follows: 20 mM citrate, 200 mM arginine at pH 5.0 20 mM citrate, 200 mM arginine at pH 6.0; 20 mM succinate, 250 mM sorbitol at pH 4.0; 20 mM histidine, 200 mM arginine at pH 6.0; 20 mM histidine, 75 mM arginine / 50 mM CaCl2at pH 6.0; 20 mM histidine, 75 mM arginine / 50 mM MgCl2at pH 6.0 Each of the six formulations shown above was evaluated either without surfactant or in the presence of 0.01% PS-80 for a total of twelve unique formulation conditions. For each formulation, OMS646 was exchanged into buffer-exchange solutions (no PS-80), concentrated, the content was measured and the samples were normalized to 175 mg / mL protein. Each formulation was then split and PS-80 was added into the appropriate samples to a final concentration of 0.01% (w / v). The formulated samples were each subjected to mechanical stress by agitation, and freeze / thaw cycling. For both types of stress, 0.5 mL of sample was transferred into four type 1 borosilicate glass vials (2.0 mL) and sealed using FluroTec® stoppers. For agitation stress, the samples were placed in a microplate shaker at 600 rpm for ~60 hours at room temperature. Agitation control samples were kept next to the shaker for the duration of the agitation stress. For freeze / thaw cycling, the samples were frozen at -80ºC for ≥60 minutes and then allowed to thaw at room temperature, for a total of 5 freeze-thaw cycles. Following stressing, samples were stored at 2-8ºC until analysis. The remaining sample was maintained at 2-8ºC as an unstressed control. Appearance, A280 measurements, DLS and SEC were performed to evaluate the impact of surfactant on OMS646 aggregation and stability. Results : Following stressing of the six OMS646 formulations, no sample showed evidence of product-related particulate matter. Protein content was essentially constant for all samples of a given formulation. Analysis of DLS data for freeze / thaw and agitation samples revealed only subtle differences between formulations and stress-types, with no clear global trends observed with regard to PS-80 inclusion. The one exception was the succinate / sorbitol pH 4.0 formulation in which inclusion of PS-80 led to high overall polydispersity (i.e., multimodal) for freeze / thaw and 5ºC control samples. This acidic formulation also showed evidence of aggregation / self-association by DLS in the absence of PS-80 upon agitation. Analysis of SEC data was performed to evaluate any aggregation and / or degradation products arising during sample stressing. The results are summarized in TABLES 5A-5D. TABLE 5A : Summary of SEC data for OMS646 formulation surfactant screening (2-8°C) Form. Buffer Excipient Additive pH PS-80 (%) Ave Total HMW (%) Ave Monomer (%) Ave Total LMW (%) Average Unprocessed Reference Sample 3.7 96.3 - 1 20 mM citrate 200 mM Arginine - 5.0 - 3.0 96.3 - 2 0.01 3.1 96.9 - 3 20 mM citrate 200 mM Arginine - 6.0 - 3.2 96.8 - 4 0.01 3.3 96.7 - 5 20 mM histidine 200 mM Arginine - 6.0 - 3.3 96.7 - 6 0.01 3.4 96.6 - 7 20 mM Succinate 250 mM Sorbitol - 4.0 - 3.2 96.6 0.2 8 0.01 3.2 96.5 0.2 9 20 mM histidine 75 mM Arginine 50 mM CaCl 2 6.0 - 3.3 96.7 - 10 0.01 3.4 96.6 - 11 20 mM histidine 75 mM Arginine 50 mM MgCl 2 6.0 - 3.4 96.6 - 12 0.01 3.5 96.5 - TABLE 5B : Summary of SEC data for OMS646 formulation surfactant screening (Freeze / Thaw) Form. Buffer Excipient Additive pH PS-80 (%) Ave Total HMW (%) Ave Monomer (%) Ave Total LMW (%) Average Unprocessed Reference Sample 3.7 96.3 - 1 20 mM citrate 200 mM Arginine - 5.0 - 3.1 96.9 - 2 0.01 3.2 96.8 - 3 20 mM citrate 200 mM Arginine - 6.0 - 3.3 96.7 - 4 0.01 3.3 96.7 - 5 20 mM histidine 200 mM Arginine - 6.0 - 3.3 96.7 - 6 0.01 3.4 96.6 - 7 20 mM Succinate 250 mM Sorbitol - 4.0 - 3.2 96.6 0.2 8 0.01 3.2 96.6 0.2 9 20 mM histidine 75 mM Arginine 50 mM CaCl 2 6.0 - 3.4 96.6 - 10 0.01 3.4 96.6 - 11 20 mM histidine 75 mM Arginine 50 mM MgCl 2 6.0 - 3.5 96.6 - 12 0.01 3.5 96.6 - TABLE 5C : Summary of SEC data for OMS646 formulation surfactant screening (25°C) Form. Buffer Excipient Additive pH PS-80 (%) Ave Total HMW (%) Ave Monomer (%) Ave Total LMW (%) Average Unprocessed Reference Sample 3.7 96.3 - 1 20 mM citrate 200 mM Arginine - 5.0 - 3.1 96.9 - 2 0.01 3.2 96.8 - 3 20 mM citrate 200 mM Arginine - 6.0 - 3.3 96.7 - 4 0.01 3.4 96.6 - 5 20 mM histidine 200 mM Arginine - 6.0 - 3.3 96.7 - 6 0.01 3.4 96.6 - 7 20 mM Succinate 250 mM Sorbitol - 4.0 - 3.3 96.5 0.2 8 0.01 3.3 96.5 0.2 9 20 mM histidine 75 mM Arginine 50 mM CaCl 2 6.0 - 3.4 96.6 - 10 0.01 3.5 96.5 - 11 20 mM histidine 75 mM Arginine 50 mM MgCl 2 6.0 - 3.5 96.5 - 12 0.01 3.5 96.5 - TABLE 5D : Summary of SEC data for OMS646 formulation surfactant screening (Agitation) Form. Buffer Excipient Additive pH PS-80 (%) Ave Total HMW (%) Ave Monomer (%) Ave Total LMW (%) Average Unprocessed Reference Sample 3.7 96.3 - 1 20 mM citrate 200 mM Arginine - 5.0 - 3.0 97.0 - 2 0.01 3.2 96.8 - 3 20 mM citrate 200 mM Arginine - 6.0 - 3.3 96.7 - 4 0.01 3.4 96.6 - 5 20 mM histidine 200 mM Arginine - 6.0 - 3.3 96.7 - 6 0.01 3.4 96.6 - 7 20 mM Succinate 250 mM Sorbitol - 4.0 - 2.8 97.0 0.2 8 0.01 3.3 96.5 0.2 9 20 mM histidine 75 mM Arginine 50 mM CaCl 2 6.0 - 3.4 96.3 0.3 10 0.01 3.5 96.5 - 11 20 mM histidine 75 mM Arginine 50 mM MgCl 2 6.0 - 3.4 96.6 - 12 0.01 3.6 96.5 - As shown above in TABLES 5A-5D, overall, the SEC data indicate that the OMS646 molecule is generally insensitive to inclusion of PS-80 and both freeze / thaw (TABLE 5B) and agitation stress (TABLE 5D), regardless of surfactant. It was observed that the worst performing OMS646 formulations were those containing divalent cation additives (CaCl2and MgCl2) where high molecular weight (HMW) material for these samples was clearly elevated relative to other samples and the lowest levels of monomer were observed. 5. Stability analysis under stressed and unstressed conditions for 28 days After narrowing the potential buffer, excipient, and surfactant combinations through the pre-formulation studies described above, citrate and histidine buffers were formulated using 200 mM arginine over the pH range 5.5 – 6.5 at high concentrations of 175 mg / mL and 200 mg / mL OMS646 to identify the most suitable formulation under both stressed (40°C) and unstressed (5°C) conditions. Arginine was included at a hypertonic level (200 mM) due to the viscosity-reducing properties at this elevated concentration. Based on statistical numerical optimization of the pre-formulation data, the most suitable OMS646 formulation was determined to be 20 mM citrate and 200 mM arginine. A panel of samples was also prepared to evaluate the impact of 0.01% PS-80 on citrate and histidine formulations. Buffer-exchange was carried out as described above, samples were concentrated and diluted to achieve the target concentrations of 175 or 200 mg / mL OMS646. During this final normalization, PS-80 was added to 0.01% for the appropriate formulations. The formulations were sterile filtered using Millipore Ultrafree-CL GV 0.22 µM sterile concentrators. One vial of each formulation was placed at 5ºC and one at 40ºC for a 28 day incubation period. The samples were analyzed at To and 28 days with regard to concentration, appearance, turbidity, osmolality, pH, DLS, DSC and viscosity. Following the 28 day incubation, it was observed that both the 175 and 200 mg / mL OMS646 succinate / sorbitol formulation stored at 40ºC developed a gel-like consistency, and thus were not analyzed. Results : With regard to the stability analysis, pH values remained stable over the duration of the study, regardless of formulation and storage condition. After 28 days, both SEC and SDS-CE analysis indicated substantial increases in LMW content for the acidic pH 5.0 and pH 4.0 formulations, eliminating these formulations from further consideration. For the pH 6.0 citrate / arginine and histidine / arginine formulated with 0.01% PS-80, most responses were nearly indistinguishable from associated surfactant-free samples. SEC, however, showed reductions in HMW content of 0.2% - 0.6% relative to surfactant-free counterpart formulations. Coupled with the apparent viscosity-reducing properties of the surfactant, polysorbate-80 (PS-80) was chosen to be included in further formulation studies. The concentration and viscosities of a total of 10 formulations were tested after 28 days at 5ºC. Representative results are shown in TABLE 6. TABLE 6 . Viscosity of Formulations after 28 days at 5ºC. Sample Formulation Concentration 28 days at 5ºC (mg / mL) Viscosity (cP) 1 20 mM Citrate, 200 mM Arginine, pH 6.0, 175 mg / mL OMS646 153.4 10.6 2 20 mM Histidine, 200 mM Arginine, pH 6.0, 175 mg / mL OMS646 151.3 12.7 3 20 mM Citrate, 200 mM Arginine, pH 6.0, 200 mg / mL OMS646 170.5 27.4 4 20 mM Histidine, 200 mM Arginine, pH 6.0, 200 mg / mL OMS646 184.2 18.1 5 20 mM Citrate, 200 mM Arginine, 0.01% PS-80, pH 6.0, 175 mg / mL OMS646 159.2 9.0 6 20 mM Histidine, 200 mM Arginine, 0.01% PS-80, pH 6.0, 175 mg / mL OMS646 156.0 7.8 7 20 mM Citrate, 200 mM Arginine, pH 5.0, 175 mg / mL OMS646 143.2 9.8 8 20 mM Histidine, 200 mM Arginine, pH 5.0, 200 mg / mL OMS646 182.4 15.9 9 20 mM Succinate, 250 mM Sorbitol, pH 4.0, 175 mg / mL OMS646 150.6 14.5 10 20 mM Succinate, 250 mM Sorbitol, pH 4.0, 200 mg / mL 184.3 18.0 As shown above in TABLE 6, higher concentration formulations displayed higher viscosities. Of considerable interest was the observation that inclusion of PS-80 led to reduction in viscosity for both citrate (10.6 vs 9.0 cP) and histidine (12.7 vs. 7.8 cP) formulations, while also preserving protein recovery. Such reductions in viscosity upon inclusion of PS-80 are beneficial, allowing for a higher concentration of OMS646 while maintaining a low viscosity that is considered to be syringeable in a clinical setting and also suitable for use in an autoinjector and other injection devices. Summary of the results The primary aim of these studies was to identify formulation components that would result in optimal chemical, physical, and structural stability of high concentration OMS646 antibody in liquid formulations. In addition, several viscosity-specific studies were carried with the goal of obtaining a final formulation with maximal OMS646 antibody concentration that could be feasibly delivered by subcutaneous administration. Several buffer types, pH conditions, excipients, and surfactant concentrations were evaluated in an iterative fashion over the course of the studies directed at evaluation of buffer systems, excipients, solubility, viscosity, and surfactant screening studies. The initial Baseline Buffer Evaluation Study tested five different buffer types (acetate, citrate, succinate, histidine, and phosphate) over the pH range 4.0 – 8.0. Analysis by DSC, DLS, and the AVIA chemical denaturation system indicated that more acidic and basic conditions were least suitable for OMS646 antibody stability. Based on the results, acetate, citrate, and histidine buffer systems were selected for further evaluation. Excipient screening evaluated the effect of NaCl, L-arginine, L-glutamate, L-proline, sucrose, and sorbitol on OMS646 antibody stability in each of the three chosen buffer systems. Citrate (pH 6.0) was carried forward alone into further studies to maximize design space for additional excipient evaluation. Only sucrose was eliminated as a potential excipient due to poor light scattering data. Solubility screening evaluated the ability of citrate (pH 5.0 and pH 6.0) formulations containing isotonic combinations of NaCl, sorbitol, arginine, glutamate, and proline to support high solution concentrations of OMS646 antibody. All formulations were concentrated in excess of 150 mg / mL OMS646 without evidence of aggregation. Succinate / arginine and succinate / glutamate formulations, however, showed evidence of precipitation / aggregation following short-term storage and were not evaluated further.Biophysical analysis of the citrate formulations showed only minor differences between excipients at pH 6.0 and only a modest reduction of HMW content in counterpart pH 5.0 formulations. Interesting data came from viscosity measurements of this subset of samples, which suggested that citrate / glutamate and succinate / sorbitol imparted the lowest viscosities. Given the similar biophysical stabilities observed between excipients and the importance of obtaining a formulation with maximum OMS646 content, additional viscosity studies were performed. These viscosity studies identified divalent cations and / or modest hypertonicity as a significant factor in reducing OMS646 antibody formulation viscosity at more neutral pH. Both citrate (pH 5.0 and 6.0) and histidine (pH 6.0) were evaluated in the presence of 200 mM arginine. Histidine pH 6.0 was also evaluated in the presence of 75 mM arginine and either 50 mM CaCl2or 50 mM MgCl2. Finally, succinate / sorbitol pH 4.0 was tested. All buffer / excipient combinations were tested either in the absence or presence of 0.01% PS-80 to determine if surfactant promoted OMS646 antibody stability under agitation and freeze / thaw stress conditions. All formulations appeared stable against the environmental stresses applied, regardless of surfactant. One striking observation was the increase in OMS646 HMW content observed by SEC for formulations containing divalent cations. Therefore, CaCl2and MgCl2were eliminated form further consideration as excipients. Succinate / sorbitol also showed reduced OMS646 antibody purity, which was mainly attributable to an apparent increase in LMW impurities. While the differences between formulation containing and lacking 0.01% PS-80 were minor, samples containing surfactant did appear to show modestly increased HMW content (~0.1%) relative to their surfactant-free counterparts. EXAMPLE 3 This Example describes a study in which three candidate highly concentrated, low viscosity OMS646 formulations, identified based on the pre-formulation studies described in Example 2, were compared with respect to syringeability. Background / Rationale : The time and force required for a manual injection (or time required for an injection using an auto-injector) are important and may impact the ease of use of the product by the end-user and thus compliance. The force required for the injection of a solution at a given injection rate via a needle of predetermined gauge and length is referred to as ‘syringeability’ (see e.g., Burckbuchler, V.; et al., Eur. J. Pharm. Biopharm. 76 (3), 351-356, 2010 ). With regard to syringeability for administration to a human subject, one generally does not want to exceed a 25N force (although there are marketed formulations more viscous than this). A 27GA needle or a 27GA thin wall needle are generally considered standard needles for subcutaneous injection of monoclonal antibodies. The 27GA thin wall needle has an ID roughly equal to a 25GA needle (smaller G numbers are bigger diameters). The following study was carried out to determine the syringeability of three candidate highly concentration low viscosity OMS646 formulations. Methods : Based on the pre-formulation studies described in Example 2, the following three candidate high concentration OMS646 formulations were selected and further studied, as shown in TABLE 7. In this example, the formulations were prepared using arginine hydrochloride, polysorbate 80 if indicated, and either trisodium citrate or histidine, with the pH being adjusted to about 5.8 to 6.0 using hydrochloric acid. TABLE 7 : Candidate high concentration OMS646 formulations Formulation Buffer / Excipients / Surfactant / pH Concentration of OMS646 Protein content 1 20 mM Citrate, 200 mM Arginine, 0.01% PS-80, pH 5.8 185 mg / mL 187.1 2 20 mM Histidine, 200 mM Arginine, 0.01% PS-80, pH 5.9 185 mg / mL 188.2 3 20 mM Citrate, 200 mM Arginine, pH 5.8 185 mg / mL 193.3 1. Osmolality and Viscosity of OMS646 candidate formulations Osmolality and viscosity of the three candidate formulations generated as shown in TABLE 7 were determined using methods described in Example 2. Fluid behavior of the formulation was considered to be non-Newtonian if the %RSD >10 over shear rates tested. The results are shown in TABLE 8. TABLE 8 . Osmolality and Viscosity Formulation Buffer / Excipients / Surfactant / pH Conc. Osmolality (mOsm / kg) Viscosity (cP) Fluid Behavior 1 20 mM Citrate, 200 mM Arginine, 0.01% PS-80, pH 5.8 185 mg / mL 473 16.1 Newtonian 2 20 mM Histidine, 200 mM Arginine, 0.01% PS-80, pH 5.9 185 mg / mL 440 15.9 Newtonian 3 20 mM Citrate, 200 mM Arginine, pH 5.8 185 mg / mL 468 21.3 Newtonian 2. Syringeability of OMS646 candidate formulations Methods: Syringeability analysis of the three OMS646 formulations was carried out with respect to average load and max load using 27 GA (1.25”), 25GA (1”) and 25GA thin-walled (1”) needles. Triplicate replicates of each formulation were each injected once. Results for the syringeability samples are averages of the triple replicates. Results : The three formulations shown in TABLE 7 (containing OMS646 at 185 mg / mL) were evaluated for their syringeability using 27GA (1.25”), 25GA thin-walled (1”), and 25GA (1”) needles. Reported results are the average of triplicate replicates. The results are shown in TABLE 9 and are graphically illustrated in FIGURE 7A and 7B. FIGURE 7A graphically illustrates the average load (lbf) of three candidate OMS646 formulations using 27GA, 25GA and 25GA thin-walled needles. FIGURE 7B graphically illustrates the maximum load (lbf) of three candidate OMS646 formulations using 27GA, 25GA and 25GA thin-walled needles. TABLE 9 . Syringeability of the candidate high-concentration OMS646 formulations Formulation Condition Average Load (lbf) Max Load (lbf) Average Load (N) Max Load (N) 1 27 GA 4.72 5.07 20.99 22.55 25GA 1.88 2.03 8.36 9.03 25GA (thin-wall) 1.27 1.36 5.65 6.05 2 27 GA 4.51 4.85 20.06 21.57 25GA 1.84 1.99 8.18 8.85 25GA (thin-wall) 1.26 1.32 5.60 5.80 3 27 GA 5.58 5.83 24.82 25.93 25GA 2.29 2.51 10.18 11.16 25GA (thin-wall) 1.50 1.60 6.67 7.11 As described above, with regard to syringeability for administration to a human subject, one generally does not want to exceed a 25N force. As shown above in TABLE 9, all three candidate high concentration OMS646 formulations have acceptable syringeability (i.e., a force not exceeding 25N) when injected through a 25GA or 25GA thin-walled syringe. Formulation #2 also has acceptable syringeability when injected through a 27G needle. The addition of PS-80 0.01% caused an unexpected improvement in syringeability. 3. SEC Analysis of OMS646 candidate formulations post-injection Size exclusion chromatography (SEC) was used to evaluate the quantity of aggregates and degradation products present in the three OMS646 candidate formulations post-injection. Briefly, an Agilent 1100 HPLC system was fitted with a G3000SWxl SEC column (Tosoh, 7.8 x 300 mm, 5 μm particle size). OMS646 samples were diluted to 2.5 mg / mL in SEC mobile phase (140 mM potassium phosphate, 75 mM potassium chloride, pH 7.0) and 20 μL of sample was injected into the HPLC column. The system was run using a flow rate of 0.4 mL / min, and eluted protein was detected by absorption at 280 nm (bandwidth 4 nm) with no reference correction. To assess system suitability, all samples were bracketed by mobile phase blank and gel filtration standard injections, and reference material was injected in duplicate at the beginning of the sequence.Percent abundances for individual and total high molecular weight (HMW) species and low molecular weight (LMW) species, in addition to percent monomer and total integrated peak area were reported. Results: The results of the SEC analysis of the high concentration OMS646 candidate formulations post-injection are shown in TABLE 10. TABLE 10 . SEC Analysis of the high-concentration OMS646 formulations post-injection Formulation Condition % Purity % HMW % LMW 1 Control 96.5 3.3 0.1 27 GA 96.4 3.5 0.2 25 GA 96.4 3.4 0.2 25GA (thin-wall) 96.4 3.4 0.2 2 Control 96.6 3.4 Not detected 27 GA 96.5 3.5 Not detected 25 GA 96.5 3.5 Not detected 25 GA (thin-wall) 96.5 3.5 Not detected 3 Control 96.5 3.4 0.2 27 GA 96.3 3.5 0.2 25 GA 96.4 3.5 0.2 25 GA (thin-wall) 96.3 3.5 0.2 These results show little or no change in purity by SEC following expulsion through the needle. Summary of Results : The results of the syringeability analysis demonstrate that all three candidate high concentration OMS646 formulations have acceptable syringeability when tested using needles suitable for subcutaneous administration and there is little or no change in purity of the OMS646 following expulsion through the needle. The addition of PS-80 0.01% provided an unexpected improvement in the syringeability of the citrate arginine-containing formulation. EXAMPLE 4 This Example describes a study that was carried out to evaluate the stability of candidate high-concentration low viscosity OMS646 antibody formulations during long-term storage. Methods : This study was carried out to evaluate the stability of high-concentration OMS646 antibody formulations for subcutaneous injection after long-term storage. Two candidate formulations were evaluated as follows: A) 20 mM citrate, 200 mM arginine, 0.01% PS-80, pH 5.8 (185 mg / mL OMS646) B) 20 mM histidine, 200 mM arginine, 0.01% PS-80, pH 5.9 (185 mg / mL OMS646) Samples were filled into 13mm, 2mL size USP Type I Schott Glass Tubing Vials (West Pharmaceuticals), with a 1.0mL sample fill, sealed with 13mm Fluorotec stoppers (West Pharmaceuticals), and capped with 13FO aluminum caps with buttons (West Pharmaceuticals or equivalent). The sample vials were stored in controlled temperature reach-in stability chambers at -75 ± 10°C, -20 ± 5°C, 5 ± 3°C, 25 ± 2°C / 60 ± 5% RH, and 40 ± 2°C / 75 ± 5%RH. A target of at least 40 sample vials per formulation were stored for the present study. Samples stored as liquid were stored in an inverted orientation, while frozen samples were stored upright. The required number of vials was pulled at the associated time points and conditions, and the samples were characterized by the following methods: Appearance by Visual Inspection, Protein Content by A280, Osmolality, SEC-HPLC, pH, and MASP-2 ELISA.The exemplary SEC-HPLC data is summarized in TABLE 11 and shows that the OMS646 antibody maintained its integrity after storage at 5oC for 6, 9 and 12 months. The ELISA data confirmed that the antibody preserved its functionality after storage at 5°C for 6, 9 and 12 months. Results : The results of this study are summarized in TABLE 11 below. TABLE 11 . Stability of Formulations as analyzed by SEC Formulation Time Point Condition Total HMW (oligomer) (%) Main Peak (monomer) (%) Total LMW (%) 185 mg / mL OMS646 20 mM Citrate 200mM Arginine 0.01% Polysorbate 80 pH 5.8 T0 NA 3.9 96.1 - 1 month -20 o C 2.5 97.5 - 5 o C 2.6 97.4 - 25 o C / 60% RH 2.7 97.3 - 2 months -20 o C 2.9 97.1 - 5 o C 3.1 96.9 - 25 o C / 60% RH 3.4 96.6 - 3 months -20 o C 2.8 97.2 - 5 o C 2.9 97.1 - 25 o C / 60% RH 3.3 96.0 0.7 6 months -20 o C 1.7 98.3 - 5 o C 1.9 98.1 - 25 o C / 60% RH 2.0 98.0 - 9 months 5 o C 3.4 96.6 - 25 o C / 60% RH 4.0 95.7 0.2 12 months 5°C 3.4 96.6 - 185 mg / mL OMS646 20 mM Histidine 200mM Arginine 0.01% Polysorbate 80 pH 5.9 T0 NA 3.8 96.2 - 1 month -20 o C 2.7 97.3 - 5 o C 2.7 97.3 - 25 o C / 60% RH 2.9 97.1 - 2 months -20 o C 2.9 97.1 - 5 o C 3.3 96.7 - 25 o C / 60% RH 3.3 96.7 - 3 months -20 o C 2.8 97.1 0.1 5 o C 3.0 96.9 0.1 25 o C / 60% RH 3.1 96.1 0.8 6 months -20 o C 1.8 98.2 - 5 o C 1.9 98.1 - 25 o C / 60% RH 2.0 98.0 - As shown in TABLE 11, little or no change in purity was observed in the samples stored up to 9 months at -20ºC or stored at 5ºC up to 12 months, the intended storage temperature. The purity of the samples stored at 25ºC was also maintained over 2 months, however, slight changes in purity at 25ºC were observed over 9 months of storage. EXAMPLE 5 An exemplary formulation containing the MASP-2 inhibitory antibody OMS646 at pH 5.8 was prepared by combining OMS646 (185 mg / mL) with citrate (20 mM), arginine (200 mM) and polysorbate 80 (0.01%). Sodium citrate dihydrate (4.89 mg / mL) and citric acid monohydrate (0.71 mg / mL) were used to prepare the citrate buffer, with hydrochloric acid and / or sodium hydroxide used to adjust the pH as needed. The viscosity of this formulation was measured with a capillary viscometer, and the results are shown in TABLE 12. There is a slight decrease in viscosity at higher shear rates, with all values being below 13 cP. TABLE 12: Viscosity of an exemplary OMS646 formulation measured at different shear rates Formulation Temperature (°C) Shear Rate (1 / s) Viscosity (cP) 185 mg / mL OMS646 20 mM Citrate 200mM Arginine 0.01% Polysorbate 80 pH 5.8 25.0 103000 12.2 25.0 156000 11.5 25.0 211000 11.0 It was determined that dosing human subjects with the exemplary 185 mg / mL OMS646 formulation described in this example (both by subcutaneous injection and intravenous administration after dilution) resulted in sustained and high degrees of lectin pathway inhibition. While the preferred embodiment of the invention has been illustrated and described, it will be appreciated that various changes to the disclosed formulations and methods can be made therein without departing from the spirit and scope of the invention. It is therefore intended that the scope of letters patent granted hereon be limited only by the definitions of the appended claims. In accordance with the foregoing, the invention features the following embodiments. 1. A stable pharmaceutical formulation suitable for parenteral administration to a mammalian subject, comprising: (a) an aqueous solution comprising a buffer system having a pH of 5.0 to 7.0; and (b) a monoclonal antibody or fragment thereof that specifically binds to human MASP-2 at a concentration of about 50 mg / mL to about 250 mg / mL, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising CDR-H1, CDR-H2 and CDR-H3 of SEQ ID NO:2 and (ii) a light chain variable region comprising CDR-L1, CDR-L2 and CDR-L3 of SEQ ID NO:3, or a variant thereof comprising a heavy chain variable region having at least 95% identity to SEQ ID NO:2 and a light chain variable region having at least 95% identity to SEQ ID NO:3; wherein the formulation has a viscosity of between 2 and 50 centipoise (cP), and wherein the formulation is stable when stored at between 2oC and 8oC for at least one month. 2. The pharmaceutical formulation of paragraph 1, wherein the concentration of the antibody in the formulation is from about 100 mg / mL to about 225 mg / mL. 3. The pharmaceutical formulation of paragraph 1, wherein the concentration of the antibody in the formulation is from about 150 mg / mL to about 200 mg / mL. 4. The pharmaceutical formulation of paragraph 1, wherein the concentration of the antibody in the formulation is from about or about 175 mg / mL to about 195 mg / mL. 5. The pharmaceutical formulation of paragraph 1 or paragraph 2, wherein the viscosity of the formulation is from about 2 cP to about 40 cP. 6. The pharmaceutical formulation of paragraph 1 or paragraph 2, wherein the viscosity of the formulation is from about 2 cP to about 30 cP. 7. The pharmaceutical formulation of paragraph 1 or paragraph 2, wherein the viscosity of the formulation is from about 2 cP to about 25 cP. 8. The pharmaceutical formulation of paragraph 1 or paragraph 2, wherein the viscosity of the formulation is from about 2 cP to about 20 cP. 9. The pharmaceutical formulation of paragraph 1 or paragraph 2, wherein the viscosity of the formulation is from about 2 cP to about 18 cP. 10. The pharmaceutical formulation of any one of paragraphs 1-9, wherein the buffer system comprises at least one pharmaceutically acceptable buffering agent having an acid dissociation constant within 2 pH units of the formulation pH. 11. The pharmaceutical formulation of any one of paragraphs 1-10, wherein the buffer system comprises at least one buffering agent selected from the group consisting of succinate, histidine and citrate. 12. The pharmaceutical formulation of paragraph 11, wherein the at least one buffering agent is histidine or citrate. 13. The pharmaceutical formulation of any one of paragraphs 1-12, wherein the at least one buffering agent is citrate. 14. The pharmaceutical formulation of paragraph 13, wherein the at least one buffering agent is sodium citrate. 15. The pharmaceutical formulation of any one of paragraphs 1-12, wherein the at least one buffering agent is histidine. 16. The pharmaceutical formulation of paragraph 15, wherein the at least one buffering agent is L-histidine. 17. The pharmaceutical formulation of paragraph 13, wherein citrate is present in the solution at a concentration of 10 mM to 50 mM. 18. The pharmaceutical formulation of paragraph 15, wherein histidine is present in the solution at a concentration of 10 mM to 50 mM. 19. The pharmaceutical formulation of any one of paragraphs 1-18, wherein the pharmaceutical formulation further comprises at least one excipient selected from the group consisting of a protein, an amino acid, a sugar, a polyol, a salt, a fatty acid and a phospholipid. 20. The pharmaceutical formulation of paragraph 19, wherein the at least one excipient is a tonicity modifying agent in a sufficient amount for the formulation to be hypertonic. 21. The pharmaceutical formulation of paragraph 20, wherein the tonicity modifying agent selected from the group consisting of an amino acid with a charged side chain, a sugar or other polyol and a salt. 22. The pharmaceutical formulation of paragraph 21, wherein the tonicity modifying agent is a sugar or other polyol and is selected from the group consisting of sucrose, trehalose, mannitol and sorbitol. 23. The pharmaceutical formulation of paragraph 21, wherein the tonicity modifying agent is a salt selected from the group consisting of NaCl or a salt of an amino acid. 24. The pharmaceutical formulation of paragraph 21, wherein the tonicity modifying agent is an amino acid with a charged side chain. 25. The pharmaceutical formulation of paragraph 24, wherein the amino acid with a charged side chain is present in the formulation at a concentration of from about 150 mM to about 300 mM. 26. The pharmaceutical formulation of paragraph 24 or 25, wherein the tonicity modifying agent is an amino acid with a negatively charged side chain. 27. The pharmaceutical formulation of paragraph 24 or 25, wherein the tonicity modifying agent excipient is an amino acid with a positively charged side chain. 28. The pharmaceutical formulation of paragraph 26, wherein the tonicity modifying agent is glutamate. 29. The pharmaceutical formulation of paragraph 27, wherein the tonicity modifying agent is arginine. 30. The pharmaceutical formulation of paragraph 29, wherein the tonicity agent is L-arginine HCl. 31. The pharmaceutical formulation of paragraph 29, wherein arginine is present in the solution at a hypertonic level of from 200 mM to 300 mM. 32. The pharmaceutical formulation of paragraph 17, wherein the solution comprises about 20 mM citrate and has a pH from about 5.5 to about 6.5. 33. The pharmaceutical formulation of paragraph 32, wherein the solution further comprises arginine at a concentration of about 200 mM. 34. The pharmaceutical formulation of paragraph 18, wherein the solution comprises about 20 mM histidine and has a pH from about 5.5 to about 6.5. 35. The pharmaceutical formulation of paragraph 34, wherein the solution further comprises arginine at a concentration of about 200 mM. 36. The pharmaceutical formulation of any one of paragraphs 1-35 wherein the solution further comprises a surfactant at a concentration from about 0.001% (w / v) and about 0.1% (w / v). 37. The pharmaceutical formulation of paragraph 36, wherein the surfactant is a nonionic surfactant. 38. The pharmaceutical formulation of paragraph 37, wherein the surfactant is a polysorbate or a poloxamer. 39. The pharmaceutical formulation of paragraph 38, wherein the surfactant is polysorbate 80. 40. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the formulation is stable when stored at between 2°C and 8°C for at least 6 months. 41. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the formulation is stable when stored at between 2°C and 8°C for at least 12 months. 42. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the viscosity is less than about 25 cP. 43. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the viscosity is less than about 20 cP. 44. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the viscosity is less than about 18 cP. 45. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the injection glide force of the formulation is about 25 Newton or less when injected through a 27GA 1.25” needle at room temperature. 46. The pharmaceutical formulation of any one of paragraphs 1-39, wherein the injection glide force of the formulation is about 20 Newton or less when injected through a 25GA 1” needle at room temperature. 47. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: about 20 mM sodium citrate, about 200mM L-arginine HCl, wherein the concentration of the antibody in the formulation is from about 175 mg / mL to about 195 mg / mL, and wherein the viscosity is less than about 25cP. 48. The pharmaceutical formulation of paragraph 47, wherein the formulation further comprises from 0.001% w / v to 0.05% w / v polysorbate 80. 49. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: about 20mM L-histidine, about 200mM L-arginine HCl, wherein the concentration of the antibody in the formulation is from about 175 mg / mL to about 195 mg / mL, and wherein the viscosity is less than about 25cP. 50. The pharmaceutical formulation of paragraph 49, wherein the formulation further comprises from 0.001% w / v to 0.05% w / v polysorbate 80. 51. The pharmaceutical formulation of any one of paragraphs 1-50, wherein the formulation is sterile. 52. The pharmaceutical formulation of any one of paragraphs 1-50, wherein the monoclonal antibody is a full length monoclonal antibody. 53. The pharmaceutical formulation of paragraph 52, wherein the antibody is a human IgG4 full length antibody. 54. The pharmaceutical formulation of paragraph 53, wherein the IgG4 comprises a mutation in the hinge region. 55. The pharmaceutical formulation of any one of paragraphs 1-54, wherein the formulation does not include sucrose or sorbitol. 56. The pharmaceutical formulation of any one of paragraphs 1-54, wherein the formulation does not include CaCl2. 57. The pharmaceutical formulation of any one of paragraphs 1-54, wherein the formulation does not include MgCl2. 58. The pharmaceutical formulation of any one of paragraphs 1-54, wherein the formulation does not include CaCl2and wherein the formulation does not include MgCl2. 59. The pharmaceutical formulation of any of paragraphs 1-54, wherein the formulation does not include a divalent cation additive. 60. The pharmaceutical formulation of any one of paragraphs 1-59, wherein the concentration of the antibody is about 185 mg / mL. 61. The pharmaceutical formulation of any one of paragraphs 1-60, wherein the formulation further comprises a hyaluronidase enzyme in an amount effective to increase the dispersion and / or absorption of the antibody following subcutaneous administration. 62. The pharmaceutical formulation of paragraph 61, wherein the formulation comprises from about 100 U / mL to about 20,000 U / mL of said hyaluronidase enzyme. 63. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: (a) polysorbate 80 at a concentration from about 0.01 to about 0.08% w / v; (b) L-arginine HCl at a concentration from about 150 mM to about 200 mM; (c) sodium citrate at a concentration from about 10 mM to about 50 mM; and (d) about 150 mg / mL to about 200 mg / mL of the antibody. 64 The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: (a) polysorbate 80 at a concentration from about 0.01 to about 0.08% w / v; (b) L-arginine HCl at a concentration from about 150 mM to about 200 mM; (c) L-histidine at a concentration from about 10 mM to about 50 mM; and (d) about 150 mg / mL to about 200 mg / mL of the antibody. 65. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: (a) polysorbate 80 at a concentration of about 0.01 w / v; (b) L-arginine HCl at a concentration of about 200 mM; (c) sodium citrate at a concentration of about 20 mM; and (d) about 175 mg / mL to about 195 mg / mL of the antibody. 66. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: (a) polysorbate 80 at a concentration of about 0.01% w / v; (b) L-arginine HCl at a concentration of about 200 mM; (c) L-histidine at a concentration of about 20 mM; and (d) about 175 mg / mL to about 195 mg / mL of the antibody. 67. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: (a) polysorbate 80 at a concentration of about 0.01% w / v; (b) L-arginine HCl at a concentration of about 200 mM; (c) sodium citrate at a concentration of about 20 mM; and (d) about 175 mg / mL to about 195 mg / mL of the antibody. 68. The pharmaceutical formulation of paragraph 1, wherein the formulation comprises: (a) polysorbate 80 at a concentration of about 0.01% w / v; (b) L-arginine HCl at a concentration of about 200 mM; (c) L-histidine at a concentration of about 20 mM; and (d) about 175 mg / mL to about 195 mg / mL of the antibody. 69. The pharmaceutical formulation of any of paragraphs 63 to 68 wherein the formulation further comprises from about 100 U / mL to about 20,000 U / mL of a hyaluronidase enzyme effective to increase the dispersion and / or absorption of the antibody following subcutaneous administration. 70. A stable aqueous pharmaceutical formulation suitable for parenteral administration to a mammalian subject, the formulation consisting essentially of: (a) polysorbate 80 at a concentration from about 0.01 to about 0.08% w / v; (b) L-arginine HCl at a concentration from about 150 mM to about 200 mM; (c) sodium citrate at a concentration from about 10 mM to about 50 mM; and (d) a monoclonal antibody or fragment thereof that specifically binds to human MASP-2 at a concentration of about 150 mg / mL to about 200 mg / mL, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising CDR-H1, CDR-H2 and CDR-H3 of SEQ ID NO:2 and (ii) a light chain variable region comprising CDR-L1, CDR-L2 and CDR-L3 of SEQ ID NO:3, or a variant thereof comprising a heavy chain variable region having at least 95% identity to SEQ ID NO:2 and a light chain variable region having at least 95% identity to SEQ ID NO:3; wherein the formulation has a pH from about 5.0 to about 7.0, a viscosity of between 2 and 50 centipoise (cP), and wherein the formulation is stable when stored at between 2oC and 8oC for at least one month. 71. A stable aqueous pharmaceutical formulation suitable for parenteral administration to a mammalian subject, the formulation consisting essentially of: (a) polysorbate 80 at a concentration from about 0.01 to about 0.08% w / v; (b) L-arginine HCl at a concentration from about 150 mM to about 200 mM; (c) L-histidine at a concentration from about 10 mM to about 50 mM; and (d) a monoclonal antibody or fragment thereof that specifically binds to human MASP-2 at a concentration of about 150 mg / mL to about 200 mg / mL, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising CDR-H1, CDR-H2 and CDR-H3 of SEQ ID NO:2 and (ii) a light chain variable region comprising CDR-L1, CDR-L2 and CDR-L3 of SEQ ID NO:3, or a variant thereof comprising a heavy chain variable region having at least 95% identity to SEQ ID NO:2 and a light chain variable region having at least 95% identity to SEQ ID NO:3; wherein the formulation has a pH from about 5.0 to about 7.0, a viscosity of between 2 and 50 centipoise (cP), and wherein the formulation is stable when stored at between 2oC and 8oC for at least one month. 72. The formulation of any of paragraphs 1-71 wherein the antibody or fragment thereof comprises a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3. 73. A sealed container containing a formulation according to any one of paragraphs 1-72. 74. A subcutaneous administration device containing the formulation of any one of paragraphs 1-72 therein. 75. A kit comprising a pre-filled container comprising the pharmaceutical formulation comprising the MASP-2 antibody of any of paragraphs 1-72 and instructions for use of the formulation. 76. The kit of paragraph 75 wherein the pre-filled container is selected from the group consisting of: a syringe, a pen injector, a sealed vial, an auto-injector and a pump device (e.g., an on-body patch pump or a tethered pump). 77. A kit comprising: (a) a first pre-filled container comprising the pharmaceutical formulation comprising the MASP-2 antibody of any of paragraphs 1-60 or paragraphs 63-72; (b) a second pre-filled container comprising an amount of hyaluronidase enzyme effective to increase the dispersion and / or absorption of the MASP-2 antibody following subcutaneous administration; and (c) instructions for use. 78. The kit of paragraph 77 wherein at least one of the first or second pre-filled container(s) is selected from the group consisting of: a syringe, a pen injector, a sealed vial, an auto-injector and a pump device (e.g., an on-body patch pump or a tethered pump). 79. A pharmaceutical unit dosage form suitable for parental administration to a human, comprising a formulation according to any of paragraphs 1-72 in a suitable container. 80. A method of treating a subject suffering from a disease or disorder amenable to treatment with a MASP-2 inhibitory antibody comprising administering a formulation of any one of paragraphs 1-72 to the subject in need thereof. 81. The method of paragraph 80, wherein the formulation is administered subcutaneously to the subject. 82. The method of paragraph 80, wherein the method further comprises administering to the subject a hyaluronidase enzyme in an amount effective to increase the dispersion and / or absorption of the antibody. 83. The method of paragraph 82, wherein the hyaluronidase enzyme is administered simultaneously with the formulation comprising the MASP-2 inhibitory antibody. 84. The method of paragraph 82 or 83, wherein the formulation comprises the MASP-2 inhibitory antibody and the hyaluronidase enzyme. 85. The method of paragraph 82, wherein the hyaluronidase enzyme is administered to the subject prior to the formulation comprising the MASP-2 inhibitory antibody. 86. The method of paragraph82, wherein the hyaluronidase enzyme is administered to the subject after the formulation comprising the MASP-2 inhibitory antibody. 87 The method of paragraph 80, wherein the formulation is administered via a pre-filled syringe containing the formulation therein. 88. A method of inhibiting MASP-2 dependent complement activation in a subject suffering from, or at risk of developing, a complement-associated disease or disorder comprising administering a formulation of any one of paragraphs 1-72 to the subject in need thereof. 89. The method of paragraph 88, wherein the formulation is administered subcutaneously to the subject. 90. The method of paragraph 79, wherein the formulation is administered via a pre-filled syringe containing the formulation therein. 91. The method of paragraph 88, wherein the subject is suffering from or at risk of developing a complement-associated disease or disorder selected from the group consisting of a thrombotic microangiopathy (TMA), a renal condition, an inflammatory reaction resulting from tissue or organ transplantation, an ischemia reperfusion injury, a complication associated with diabetes, a cardiovascular disease or disorder, an inflammatory gastrointestinal disorder, a pulmonary disorder, an ophthalmic disease or disorder, and disseminated intravascular coagulation. 92. The method of paragraph 91, wherein the thrombotic microangiopathy is atypical hemolytic syndrome (aHUS). 93. The method of paragraph 91, wherein the thrombotic microangiopathy is associated with hematopoietic stem cell transplant. 94. The method of paragraph 91, wherein the renal condition is IgA nephropathy. 95. The method of paragraph 91, wherein the renal condition is lupus nephritis. 96. A method of inhibiting MASP-2 dependent complement activation in a subject suffering from, or at risk of developing, a complement-associated disease or disorder comprising diluting a formulation of any one of paragraphs 1-72 into a pharmaceutically-acceptable diluent and administering the diluted formulation systemically to the subject in need thereof. 97. The method of paragraph 96, wherein the diluted formulation is administered intravenously to the subject. 98. The method of paragraph 96, wherein the subject is suffering from or at risk of developing a complement-associated disease or disorder selected from the group consisting of a thrombotic microangiopathy (TMA), a renal condition, an inflammatory reaction resulting from tissue or organ transplantation, an ischemia reperfusion injury, a complication associated with diabetes, a cardiovascular disease or disorder, an inflammatory gastrointestinal disorder, a pulmonary disorder, an ophthalmic disease or disorder, and disseminated intravascular coagulation. 99. The method of paragraph 98, wherein the thrombotic microangiopathy is atypical hemolytic syndrome (aHUS). 100. The method of paragraph 98, wherein the thrombotic microangiopathy is associated with hematopoietic stem cell transplant. 101. The method of paragraph 98, wherein the renal condition is IgA nephropathy. 102. The method of paragraph 98, wherein the renal condition is lupus nephritis. 103. A pharmaceutical composition for use in treating a patient suffering from, or at risk for developing a MASP-2-dependent complement-associated disease or disorder, wherein the composition is a sterile, single-use dosage form comprising from about 350mg to about 400mg of MASP-2 inhibitory antibody, wherein the composition comprises about 1.8mL to about 2.2 mL of a 185mg / mL antibody formulation, wherein the antibody comprises (i) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and (ii) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3, and wherein the composition is stable when stored at between 2°C and 8°C for at least six months. 104. The composition of paragraph 103, wherein composition comprises a buffer system having a pH of 5.0 to 7.0. 105. The composition of paragraph 104, wherein the buffer system comprises at least one pharmaceutically acceptable buffering agent selected from the group consisting of succinate, histidine and citrate. 106. The composition of paragraph 103, wherein the composition comprises from 1.8mL to 2.2 mL of a 185 mg / mL MASP-2 inhibitory antibody formulation of any one of paragraphs 1-72. 107. The composition of any one of paragraphs 103-107, wherein the MASP-2 dependent complement-associated disease or disorder is aHUS. 108. The composition of any one of paragraphs 103-107, wherein the MASP-2 dependent complement-associated disease or disorder is HSCT-TMA. 109. The composition of any one of paragraphs 103-107, wherein the MASP-2 dependent complement-associated disease or disorder is IgAN. 110. The composition of any one of paragraphs 103-107, wherein the MASP-2 dependent complement-associated disease or disorder is Lupus Nephritis (LN). While the preferred embodiment of the invention has been illustrated and described, it will be appreciated that various changes can be made therein without departing from the spirit and scope of the invention. Manufacturing process, tools and methods for MASP-2 inhibitory antibody with low viscosity and high concentration References to similar patent applications The present application claims the benefit of U.S. Provisional Application No. 62 / 382,156, filed on 06 / 10 / 1395, which is incorporated herein by reference in its entirety. Field of invention The present invention relates to compositions of MASP-2 inhibitory antibodies with low viscosity and high concentration, devices including therapeutic methods using the compositions and devices for inhibiting the deleterious effects of complement activation. Announcement regarding sequence cataloging The sequence listing for the present application is provided in text form instead of a paper version and is used herein with attribution. The file name containing the sequence listing is as follows: MP_1_0261_PCT_SequenceListing_20170809_ST25. The file size is 17KB and was created on 05 / 18 / 1396 and submitted via EFS-Web along with the submission of the description of the invention. Background Antibody-based therapy is usually administered on a regular basis and often requires injections of several milligrams / kg of antibody. A preferred form of delivery for the treatment of chronic diseases is the outpatient administration of high doses (several milligrams / kg) of monoclonal antibodies via subcutaneous (SC) injection (Stockwin and Holmes, Expert Opin Biol Ther 3:1133-1152 (2003); Shire et al., J Pharm Sci 93:1390-1402 (2004)). Highly concentrated therapeutic antibody formulations are popular because they reduce the volume of material injected or the number of injections, which ultimately results in greater patient comfort and less discomfort. In addition, such lower volumes allow for the delivery of doses of a therapeutic monoclonal antibody in a packaged, single-dose form via syringes ready for self-administration. SC injection using a pre-filled syringe or automated injection technology allows the patient to inject at home, increasing patient confidence and compliance with the doctor's prescriptions. However, the formulation of high protein concentrations poses challenges in terms of physical and chemical stability of the protein, as well as its formulation, storage, and delivery (Wang et al., J of Pharm Sci vol 96(1):1-26, (2007)). A major challenge in the formulation of high protein concentrations is the viscosity resulting from the solution concentration. At different protein concentrations, viscosity varies significantly as a function of the formulation. In particular, monoclonal antibodies are known to have unique and diverse concentration-viscosity properties, with a significant increase in viscosity as the monoclonal antibody concentration increases (see eg, Connolly BD et al., Biophysical Journal vol 103:69-78, (2012)). Another challenge in liquid formulations with high concentrations of monoclonal antibodies is the physical stability of the protein (Alford et al., J. Pharm Sci 97:3005-3021 (2008); Salinas et al., J Pharm Sci 99:82-93 (2010); Sukumar et al., Pharm Res 21:1087-1093 (2004)).Therefore, the high viscosity of highly concentrated monoclonal antibody formulations, coupled with the potential for reduced stability, can pose challenges in their manufacturing process as products suitable for subcutaneous and / or intravenous delivery. The helper antibody system plays an important role in the inflammatory response and is activated as a result of tissue damage or microbial infection. Helper antibody activation must be carefully regulated to selectively target invading microorganisms and prevent damage to self tissues (Ricklin et al., Nat. Immunol. 11:785-797, 2010). It is currently accepted that the helper antibody system can be activated through different pathways, including the classical pathway, the lectin pathway, and the alternative pathway. The classical pathway is often activated by a combination of host antibodies that have bound to a foreign particle (e.g., an antigen) and, therefore, requires that the antigen has been previously encountered in order to mount an antibody response. Since activation of the classical pathway requires prior exposure to the host immune system, the classical pathway is considered part of the adaptive immune system. In contrast, both the lectin and alternative pathways do not require prior exposure and are considered part of the innate immune system. The lectin pathway, a major pathway for the activation of helper antibodies, has been shown to require the mannan-binding lectin-dependent serine protease-2 (MASP-2) (Vorup-Jensen et al., J. Immunol 165:2093-2100, 2000; Ambrus et al., J Immunol. 170:1374-1382, 2003; Schwaeble et al., PNAS 108:7523-7528, 2011). Importantly, MASP-2 inhibition does not disrupt the classical antibody-dependent helper antibody activation pathway, which is a critical part of the adaptive immune response to adjuvant. As disclosed in U.S. Patent Application No. 9,011,860 (Omeros Corporation), and referred to herein as OMS646, a fully human monoclonal antibody targeting human MASP-2 has been generated that binds with high affinity to human MASP-2 and blocks the activity of the lectin pathway adjuvant antibody and is therefore useful for the treatment of various diseases and disorders associated with lectin pathway adjuvant antibody. As disclosed in patent applications Nos. 7,919,094, 8,840,893, 8,652,477, 8,951,522, 9,011,860, 9,644,035 and patents Nos. US2013 / 0344073, US2013 / 0266560, US 2015 / 0166675, US2017 / 0189525, and pending patents Nos. 15 / 476,154, 15 / 347,434, 15 / 470,647, 62 / 315,857, 62 / 275,025 and 62 / 527,926 (all owned by Omeros Corporation, all of which are incorporated herein by reference) (End) It has been reported that MASP-2-dependent antibody activation is known to be a contributing factor in the pathogenesis of numerous acute and chronic diseases. Therefore, there is a need for a stable, high-concentration, low-viscosity formulation of MASP-2 monoclonal antibody that is suitable for injection (e.g., subcutaneously) to treat individuals with disorders and diseases mediated by MASP-2 pathway antibodies. Summary In one aspect, the present disclosure provides a stable pharmaceutical composition suitable for injection into a mammalian subject, comprising: a) an aqueous solution comprising a buffer system having a pH of 5.0 to 7.0, and b) a monoclonal antibody or portion thereof that binds exclusively to human MASP-2 at concentrations of about 50 mg / mL to 250 mg / mL, wherein the monoclonal antibody or portion thereof comprises: 1) a heavy chain variable region comprising CDR-H1, CDR-H2, and CDR-H3 of SEQ ID NO: 2 and 2) a light chain variable region comprising CDR-L1, CDR-L2, and CDR-L3 of SEQ ID NO: 3 or variants thereof comprising a heavy chain variable region having at least 95% similarity to SEQ ID NO: 2 and a light chain variable region having at least 95% similarity to SEQ ID NO: 3, such that the viscosity of the composition is between 2 and 50 poise. (cP) and such that the composition is stable when stored at a temperature between 2 and 8 degrees Celsius for at least one month. In some embodiments, the concentration of antibody in the composition is from about 150 mg / mL to 200 mg / mL. In some embodiments, the viscosity of the composition is less than 25 cP.In some embodiments, the buffering system comprises histidine. In some embodiments, the buffering system comprises citrate. In some embodiments, the formulation comprises an additive such as a resiliency modifier in an amount sufficient to render the composition hypertonic. In some embodiments, the composition also comprises a surfactant. In some embodiments, the composition also comprises an abgenzyme enzyme (hyaluronic acid-translating neutralizing enzyme) in an amount sufficient to enhance dispersion and / or absorption of the antibody following subcutaneous injection. In another aspect, the composition is contained within a subcutaneous injection device, such as a pre-filled syringe. In another aspect, the present invention provides a kit comprising a pre-filled syringe containing the composition. In another aspect, the present invention provides a pharmaceutical composition for use in treating patients suffering from or at risk of developing diseases caused by MASP-2, wherein the composition, in a single sterile dose, comprises about 350 mg to 400 mg (i.e., 350 mg, 360 mg, 370 mg, 380 mg, 390 mg, or 400 mg) of a MASP-2 inhibitory antibody, wherein the composition comprises about 1.8 ml to about 2.2 ml (i.e., 1.8 ml, 1.9 ml, 2.0 ml, 2.1 ml, or 2.2 ml) of a 185 mg / ml antibody composition as disclosed herein, wherein said antibody or fragment thereof comprises: 1) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO: NO:2 and 2) a light chain variable region containing the amino acid sequence of SEQ ID NO:3, such that the compound remains stable when stored at a temperature between 2 and 8 degrees Celsius for at least six months.In some embodiments, the MASP-2-induced disease is selected from the group consisting of: aHUS, HSCT-TMA, lupus nephritis (LN), and IgAN. In another aspect, the present invention provides a method for treating individuals with diseases treatable with MASP-2 inhibitory antibodies, comprising administering a composition comprising a MASP-2 antibody, as described herein. Description of shapes Other aspects and many other advantages of the present invention will become more apparent from the description of the present invention with reference to the figures. The figures attached to the description of the present invention are: Figure 1A: The amount of lectin-mediated membrane attack covalent (MAC) precipitation in the presence of different amounts of human MASP-2 monoclonal antibody (OMS646) indicates that OMS646 inhibits lectin-mediated MAC precipitation with an IC50 value of approximately 1 nM, as described in Example 1. Figure 1B: Shows the amount of MAC precipitation mediated by the classical pathway in the presence of different amounts of human MASP-2 monoclonal antibody (OMS646), indicating that OMS646, as described in Example 1, does not prevent MAC precipitation mediated by the classical pathway. Figure 1C: Shows the amount of alternative pathway-mediated MAC precipitation in the presence of different amounts of human MASP-2 monoclonal antibody (OMS646), indicating that OMS646 does not prevent alternative pathway-mediated MAC precipitation as described in Example 1. Figure 2A: Shows the results of Dynamic Light Scattering (DLS) analysis for the additive composition OMS646 and indicates the overall particle diameters found in compositions containing different additive samples corresponding to Sample 2. Figure 2B: Shows the results of Dynamic Light Scattering (DLS) analysis for the additive composition OMS646 and indicates the overall polydispersity in compositions containing different additive samples according to Example 2. Figure 3: Results of spectral viscosity analysis of OMS646 concentrations in different compositions as measured at pH 5.0 and pH 6.1 in sample 2. Figure 4: Shows the percentage of protein recovery after buffer exchange to investigate the solubility / viscosity of OMS646 in the compositions according to Example 2. Figure 5: Viscosity (determined by exponential fitting of viscosity data) versus protein concentration to investigate the solubility / viscosity of OMS646 in compositions according to Example 2. Figure 6: Shows the concentration-equilibrated protein viscosity data to investigate the solution viscosity of OMS646 in the compositions according to Example 2. Figure 7A: Average value (1bf) of three OMS646 samples in syringability testing using 27 GA (1.25”), 25GA (1”) and 25GA thin wall (1”) according to sample 3. Figure 7B: Shows the maximum value (1bf) of three OMS646 samples in the syringability test using 27 GA (1.25”), 25GA (1”), and 25GA thin wall (1”) according to sample 3. Description of sequence cataloging SEQ ID NO:1: Human MASP-2 protein (mature) SEQ ID NO:2: OMS646 polypeptide heavy chain variable region (VH) SEQ ID NO:3: OMS646 polypeptide light chain variable region (VL) SEQ ID NO:4: OMS646 polypeptide complete IgG4 heavy chain mature heavy chain SEQ ID NO:5: Complete light chain OMS646 polypeptide SEQ ID NO:6: DNA encoding the complete heavy chain polypeptide OMS646 SEQ ID NO:7: DNA encoding the complete light chain polypeptide OMS646 Detailed description 1. Definitions All terms used herein have the same meaning as understood by those skilled in the art unless expressly stated otherwise herein. The following definitions are provided to provide clarity regarding terms used in the specification and claims of the present invention. Standard and well-known techniques are used for recombinant DNA, oligonucleotide synthesis, and tissue culture and transformation (e.g., electroporation, lipofection). Enzyme reaction and purification techniques are performed according to manufacturer's instructions or methods known in the art and will be described herein. These techniques and methods are largely based on conventional methods known in the art and are described herein by specific and general references. Some of these references include: Sambrook et al., 2001, MOLECULAR CLONING: A LABORATORY MANUAL, 3d ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Current Protocols in Molecular Biology (Greene Publ. Assoc. Inc. & John Wiley & Sons, Inc., NY, NY); Current Protocols in Immunology (Edited by: John E. Coligan, Ada M. Kruisbeek, David H. Margulies, Ethan M. Shevach, Warren Strober 2001 John Wiley & Sons, NY, NY) or other well-known sources and works.The list of relevant terms and laboratory processes and techniques, molecular biology, analytical chemistry, synthetic organic chemistry, and medicinal and therapeutic chemistry used herein are used in the common sense of the field unless otherwise expressly stated. In the cases of molecular biology, microbiology analysis, chemical synthesis and chemistry, pharmaceutical solutions, compositions, drug delivery, and patient treatment, well-known techniques are also used. The term "pharmaceutical composition" refers to a composition that is in a form that allows the biological activity of the active agent (e.g., MASP-2 inhibitory antibody) to be effective in therapy. The composition also does not contain any additional ingredients that are unacceptably toxic to the subject. The compositions are sterile. In some cases, the pharmaceutical composition is suitable for injection, e.g., subcutaneously. The term "MASP-2" refers to mannan-binding lectin-related serine protease-2. The human (mature) MASP-2 protein is designated as SEQ ID NO:1. The term "MASP-2-dependent antibody activation" refers to the activation of the lectin pathway by MASP-2 that occurs under physiological conditions (i.e., in the presence of C++), leading to the formation of the C3 convertase of the lectin pathway, C4b2a, and the accumulation of the C3 cleavage product, C3b, followed by the C5 convertase, C4b2a(C3b)n. The "lectin pathway" refers to the activation of adjuvant antibodies that occurs through the exclusive binding of serum and non-serum carbohydrate-binding proteins, including mannan-binding lectin (MBL), CL-11, and ficolins (H-ficolin, M-ficolin, or L-ficolin). The term "classical pathway" refers to the activation of helper antibodies, which is initiated by an antibody bound to foreign particles and requires binding of the recognition molecule C1q. The term "MASP 2 inhibitory antibody" refers to an antibody or antigen-binding fragment that binds to MASP 2 and effectively inhibits the activation of a MASP 2-dependent complement antibody (e.g., OMS646). The MASP-2 inhibitory antibodies used in the method of the present invention can reduce MASP 2-dependent complement activity by more than 20%, e.g. more than 30%, or e.g. more than 40%, or e.g. more than 50%, or e.g. more than 60%, or e.g. more than 70%, or e.g. more than 80%, or e.g. more than 90%, or e.g. more than 95%. The term "OMS646 monoclonal antibody" refers to a monoclonal antibody comprising CDR-H1, CDR-H2 and CDR-H3 of the heavy chain variable region amino acid sequence set forth as SEQ ID NO:2, and comprising CDR-L1, CDR-L2 and CDR-L3 of the light chain variable region amino acid sequence set forth as SEQ ID NO:3. This particular antibody is an example of a MASP-2 inhibitory antibody that specifically binds to MASP-2 and prevents MASP-2-dependent adjuvant antibody activation. The term "monoclonal antibody" refers to a homogeneous antibody population in which the monoclonal antibody contains amino acids (natural and unnatural) that selectively bind an epitope. Monoclonal antibodies are highly specific and selective in their antigenic targeting. Monoclonal antibodies include not only intact monoclonal antibodies and full-length monoclonal antibodies, but also fragments thereof (e.g., Fab, Fab', F(ab')2, Fv), single chain (ScFv), variants thereof, secreted proteins comprising an antibody moiety with an antigen-binding moiety, humanized antibodies, chimeric monoclonal antibodies, and any other modified immunoglobulin molecule that contains an antigen-binding moiety (epitope-recognizing moiety) and is capable of binding to an epitope. This is not meant to be limited to the source of the antibody or the method by which it was made (e.g., hybridoma, bacterivorous selection, recombinant expression, transgenic animal, etc.). The term includes all immunoglobulins as well as their fragments, etc., described above under the definition of "antibody." The term "antibody fragment" refers to a portion derived from or related to a complete antibody, such as, for example, MASP-1, MASP-2 or MASP-3 antibodies, which generally also includes antigen-binding regions or variants thereof. Examples of antibody fragments include Fab, Fab', F(ab)2, F(ab')2 and Fv, scFv fragments, dibodies, linear antibodies, single-chain antibodies, single-chain antibody molecules and multispecific antibodies composed of antibody fragments. A single-chain Fv antibody fragment, or "scFv", contains the VH and VL regions of an antibody, where these regions are present in a single polypeptide chain. Typically, the Fv polypeptide also contains a polypeptide linker between the VH and VL regions, which allows the scFv to form the desired structure for binding to the antigen. The term "CDR region" or "CDR" refers to the hypervariable regions of the heavy and light chains of immunoglobulins as described by Kabat and colleagues (Kabat, EA et al., (1991) Sequences of Proteins of Immunological Interest, 5thEdition and later editions). An antibody typically contains three heavy chain CDRs and three light chain CDRs. The term CDR or CDRs is used herein to indicate one or more or all of these regions, which contain the major portion of the amino acid residues that are involved in binding the antibody to the antigen epitope it recognizes. The term "exclusive binding" refers to the ability of an antibody to selectively bind a specific analyte present in a homogeneous mixture of different analytes. In some embodiments of the present invention, a mutually exclusive binding discriminates between desired and undesired analytes present in a sample, and this discrimination in some embodiments is greater than about 10 to 100 fold or more (e.g., greater than 1000 to 10,000 fold). In some embodiments of the invention, the affinity between the binding agent and the analyte when exclusively converted to a binding agent / analyte complex is represented by the symbol KD (dissociation constant) of less than about 100 nM, or less than 50 nM, or less than 25 nM, or less than about 25 nM, or less than about 5 nM, or less than about 1 nM. The term "isolated antibody" refers to an antibody that has been identified and / or recovered and / or purified and isolated from a component of its natural environment or cell culture expression system. In preferred embodiments, 1) the antibody is purified to greater than 95% by weight and preferably greater than 99% by weight as determined by a method suitable for measuring protein concentration, such as, the Lowry method or absorbance at OD280. 2) it is purified to a degree sufficient to obtain at least 15 precipitates of the N-terminal or internal amino acid sequence using a spin-cup sequencer or 3) it is purified to a degree sufficient to be resolved by SDS-PAGE under reducing or non-reducing conditions using Coomassie blue or, preferably, silver staining. Typically, an isolated antibody for use in the compositions described herein is prepared by at least one of the above purification methods. The amino acid residues used here are as follows: alanine (Ala; A), asparagine (Asn; N), aspartic acid (Asp; D), arginine (Arg; R), cysteine ​​(Cys; C), glutamic acid (Glu; E), glutamine (Gln; Q), glycine (Gly; G), histidine (Hush), isoleucine (Ilia), leucine (Lull), lysine (Lys; K), methionine (Met; M), phenylalanine (Phe; F), proline (Pro; P), serine (Ser; S), threonine (Thr; T), tryptophan (Trp; W), tyrosine (Tyr; Y), and valine (Val; V). In the most general sense, naturally occurring amino acids can be divided into specific groups based on the chemical properties of the amino acid side chain. "Hydrophobic" amino acids are one of the following: Ile, Leu, Met, Phe, Trp, Tyr, Val, Ala, Cys, Pro. "Hydrophilic" amino acids are one of the following: Gly, Asn, Gln, Ser, Thr, Asp, Glu, Lys, Arg, His. Amino acids can also be divided into the following subgroups: "Hydrophilic uncharged" amino acids are: Ser, Thr, Asn, Gln. "Acidic" amino acids are Glu or Asp. "Basic" amino acids are Lys, Arg, or His. The term "protective amino acid substitution" as used herein means a substitution between amino acids in any of the following groups: 1) glycine, alanine, valine, leucine and isoleucine, 2) phenylalanine, tyrosine and tryptophan, 3) serine and threonine, 4) aspartite and glutamate, 5) glutamine and asparagine, and 6) lysine, arginine and histidine. The term "subject", as used herein, means all mammals, including humans, apes, dogs, cats, sheep, goats, cattle, rabbits, pigs, and rodents. The term "pharmaceutically acceptable" in relation to an additive in a pharmaceutical composition means that the additive is suitable for use in a human subject. The term "subcutaneous injection" (or subcutaneous - translator) means injecting the compound beneath the entire layer of the subject's skin. The term "buffer" means a buffered solution that resists changes in pH due to the action of its acid-based covalent components. The buffer of the present invention has a pH of about 4 to 8, preferably about 5 to 7; and most preferably, a pH in the range of 5.5 to 6.5. Examples of buffers that control pH in this range include: acetate (e.g., sodium acetate), succinate (e.g., sodium succinate), gluconate, histidine, citrate, and other organic acid buffers. A "buffering agent" is a compound used to produce buffered solutions. The term "histidine" includes exclusively L-histidine unless explicitly stated otherwise. The term "isotonic" refers to a compound whose osmotic pressure is essentially the same as that of human blood. The osmotic pressure of isotonic compounds is generally from about 250 to 350 mOsmol / KgH20. For example, isotonicity can be measured using vapor pressure or freezing point osmometry. The term "hypertonic" means a mixture with an osmotic pressure higher than that of a human (e.g., greater than 350 mOsm / KgH20). The term "tonicity adjusting agent" means an agent that is pharmaceutically suitable for making a composition isotonic, or in some cases, hypertonic. The term "sterile" means a pharmaceutical product that is aseptic or free from bacteria, fungi, and other microorganisms, which can be achieved by any suitable means, for example, through a formulation that has been manufactured or filled aseptically, or through sterile filters, before or after the formulation and filling of the formulation. The term "stable composition" refers to the maintenance of the initial level of purity of a pharmaceutical composition over time. In other words, if the formulation is at least 95% pure in terms of the antibody type (e.g., MASP-2 inhibitory antibody) at time 0, such as at least 96% pure, at least 97% pure, at least 98% pure, or at least 99% pure, stability refers to how well and for how long this purity is maintained (e.g., without the formation of other variants such as isolated fractions (LMW) or aggregates of pure variants (HMW)). A composition can be called stable if its purity does not significantly decrease when stored for a specified period of time, such as at least 6 months, at least 9 months, at least 12 months, or at least 24 months at 2 to 8°C. By "not significantly reduced" is meant that the purity of the compound decreases by less than 5%, such as less than 4% or less than 3% or less than 2% or less than 1% over any period of time (e.g., more than 6 months, more than 9 months or more than 12 months or more than 24 months).In one embodiment, the composition is stable at a temperature of about 6 to 8°C for at least 6 months. In another preferred embodiment, the composition is stable at a temperature of about 6 to 8°C for at least one year or at least two years. In another embodiment, the MASP-2 inhibitory antibody is stable if, after storage at a temperature of 2°C to 8°C for at least one month or at least six months or at least 12 months, the composition remains at least 95% monomeric as determined by SEC-HPLC. The term "preservative" refers to a compound that can be used in a composition to substantially reduce the growth of bacteria or contamination. Non-limiting examples of possible preservatives include: octadecyldimethylbenzyl ammonium chloride, hexamethonium chloride, benzalkonium chloride (a mixture of alkylbenzyldimethylammonium chlorides in which the alkyl groups are long chain compounds), and benzalkonium chloride. Other types of preservatives include aromatic alcohols such as phenol, butyl, and benzyl alcohol, alkyl parabens such as methyl or propyl paraben, catechol, resorcinol, cyclohexanol, 3-pentanol, and m-cresol. The term "additive" means a neutral substance in a composition that adds a beneficial physical property to the composition, such as increasing protein stability and / or reducing viscosity. Examples of suitable additives include proteins (e.g., serum albumin), amino acids (e.g., aspartic acid, glutamic acid, lysine, arginine, glycine, and histidine), saccharides (e.g., glucose, sucrose, maltose, and trehalose), polyols (e.g., mannitol and sorbitol), fatty acids, and phospholipids (e.g., alkyl sulfonates and caprylate). The phrase "substantially free" means that either no substance is present or only a very small amount of a substance is present in the mixture that does not significantly affect the properties of the mixture. If it is stated that a substance is not present at all in the mixture, it means "in an undetectable amount." The term "viscosity" means the degree of resistance of a fluid to deformation either by shear stress or by tensile stress. It can be evaluated using a viscometer (e.g., a ball-roll viscometer) or rheometer. The measurement of viscosity (centipoise, cP) is that at about 25 °C with a shear rate in the range of 100,000 to 250,000 1 / s, unless proven otherwise. The term "injectable administration" means a method other than the oral route and involves the injection of a dose into the body by means of a syringe or other mechanical device such as an injection pump. Routes of administration include intravenous, intramuscular, subcutaneous, and intraperitoneal routes. Subcutaneous injection is the preferred route of administration. The term "treatment" refers to therapeutic and / or prophylactic or preventive measures. Those in need of treatment include those who are currently suffering from a disease, as well as those who need to be prevented from developing the disease. Hence, the patient being treated here may be diagnosed with the disease or may be susceptible or vulnerable to the disease. The term "effective amount" refers to the amount of a substance that produces the desired effect. In the case of pharmaceutical substances, this amount means the amount of active substance to treat a disease in a patient. In the case of the content of pharmaceutical compounds, for example, the enzyme hyaluronidase, the effective amount is the amount necessary to enhance the dispersion and absorption of the MASP-2 inhibitory antibody injected into the patient, such that the MASP-2 inhibitory antibody can act in an effective manner of treatment, as described above. The term "about" as used herein means that the amount given may vary somewhat, for example, the amounts may vary within ±10%, more preferably within ±5%, or most preferably within ±2%. For example, the phrase "a pharmaceutical formulation containing about 200 mg / mL of MASP-2 inhibitory antibody" means that the composition may contain from 180 mg / mL to 220 mg / mL of MASP-2 inhibitory antibody (e.g., OMS646). Where a range or range is mentioned, the endpoint is also intended to be within that range, unless otherwise expressly stated or indicated in the terms. The singular definite articles "a", "an" and "the", as used herein, include the plural unless expressly stated otherwise. Thus, for example, reference to the phrase "an adjuvant" includes a number of adjuvants and their equivalents familiar to those skilled in the art, "an agent" includes an agent as well as one or more agents, reference to "an antibody" includes multiple antibodies, and reference to a "framework region" means one or more framework regions familiar to those skilled in the art. Each of the embodiments presented herein should be considered more or less true of the other embodiments unless expressly stated otherwise. It is our belief that each of the embodiments discussed herein can be used with any method, package, reagent or combination of the present invention or vice versa. Furthermore, the combination of the present invention can also be used to achieve the methods of the present invention. II. Overview of the invention The present disclosure provides a stable pharmaceutical composition comprising a MASP-2 inhibitory antibody with low viscosity and high concentration that is suitable for injectable administration (e.g., subcutaneous injection) as well as for dilution prior to intravenous injection. Therapeutic antibody compositions with high concentrations are desirable because they reduce the volume of material injected or the number of injections, ultimately resulting in greater patient comfort and less discomfort. In addition, such lower volumes allow for the delivery of doses of a therapeutic monoclonal antibody in a packaged, single-dose form via syringes ready for self-administration by the patient. The high-concentration, low-viscosity compositions disclosed in the present disclosure comprise an aqueous solution containing a buffer system with a pH of 4.0 to 8.0, preferably pH 5.0 to 7.0, and a MASP-2 inhibitor monoclonal antibody (e.g., OMS646) or antigen-binding fragment thereof at a concentration of about 50 mg / mL to about 250 mg / mL.In a preferred embodiment of the present invention, the MASP-2 inhibitory antibody (e.g., OMS646) is present in high-concentration formulations suitable for subcutaneous injection at a concentration of about 100 mg / mL to 250 mg / mL, and in certain embodiments, the MASP-2 inhibitory antibody (e.g., OMS646) is present in high-concentration formulations at a concentration of about 150 mg / mL to 200 mg / mL, including about 175 mg / mL to about 195 mg / mL, such as about 185 mg / mL. In various embodiments, the pharmaceutical compositions, in addition to the high concentration MASP-2 inhibitory antibody and buffer system, comprise one or more additives such as a tonicity modifier (e.g., an amino acid with a charged side chain), and optionally a nonionic surfactant. In some embodiments, the pharmaceutical composition according to the present disclosure further comprises the enzyme hyaluronidase. A significant advantage of the high concentration MASP-2 inhibitory antibody drug compositions according to the present invention is their low viscosity and high protein concentration. As is known to those skilled in the art, high viscosity in monoclonal antibody drug compositions with concentrations ≥100 mg / mL can interfere with their manufacturing process as products for subcutaneous and / or intravenous injection. Therefore, low viscosity drug compositions are more desirable due to ease of manufacturing, such as processes such as processing, filtering, and filling. As described in Examples 2 and 3 herein, the compositions introduced in the present disclosure comprise 100 to 200 mg / mL of MASP-2 inhibitory antibody (OMS646) with a very low viscosity that falls within the following range: very low viscosity, i.e., less than about 50 cP, such as between 2 cP and 50 cP, such as between 2 cP and 40 cP, such as between 2 cP and 30 cP, or between 2 cP and 25 cP, or between 2 cP and 20 cP, or between 2 cP and 18 cP. In addition, the low viscosity, high concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention allows for the injection of the pharmaceutical composition through standard syringes and needles, automatic injection devices and microinfusion devices known in the art. As described in Example 3, the low viscosity, high concentration MASP-2 inhibitory antibody pharmaceutical composition according to what is described herein is easily inserted into the syringe and has good injectability and for these reasons is very suitable for subcutaneous injection. Absorption in the syringe and injectability are two very important factors in the production of pharmaceutical compositions that are produced for injectable use such as subcutaneous or intravenous injection and also allow for intramuscular or subcutaneous injection using thin needles such as 29GA regular or thin wall, 27GA (1.25”) regular or thin wall, 25GA (1”) regular or thin wall.In some cases, the low viscosity of the MASP-2 inhibitory antibody pharmaceutical composition as described herein allows for the injection of a reasonable volume (e.g., 1-3 cc) of the composition, thereby delivering a suitable amount of MASP-2 inhibitory antibody (OMS646) in a single injection at a single site. Another significant advantage of the composition disclosed herein is that, as described in the stability studies in Examples 2 and 4, the MASP-2 inhibitory antibody with low viscosity and high concentration (e.g., ≥ 100 mg / mL to 200 mg / mL) remains stable at a temperature of at least 2 to 8°C for at least 30 days, up to at least 9 months, or up to 12 months or more. The present invention also provides a method for preparing a pharmaceutical composition of MASP-2 inhibitory antibody with low viscosity and high concentration, comprising said composition, therapeutic kits comprising the composition, and therapeutic methods using the composition, packages and kits for treating a subject suffering from or at risk of developing a disease caused by MASP-2-mediated antibody activation. MASP-2 inhibitory antibody As described herein, the present invention relates to compositions comprising monoclonal antibodies that bind specifically to MASP-2 and inhibit the activation of a helper antibody by MASP-2 or an antigen-binding portion thereof. In certain embodiments, the MASP-2 inhibitory antibody or antigen-binding portion thereof, for use in the claimed composition of this invention, is a MASP-2 inhibitory antibody designated OMS646, disclosed in WO2012 / 151481 (which is incorporated herein by reference) comprising a heavy chain polypeptide comprising the amino acid sequence of SEQ ID NO: 2 and a light chain polypeptide comprising the amino acid sequence of SEQ ID NO: 3. As described in WO2012 / 151481 and illustrated in Example 1, OMS646 binds exclusively and with high affinity to human MASP-2 and is capable of inhibiting antibody-mediated activation of the lectin pathway.In some embodiments, the MASP-2 inhibitory antibody or antigen-binding portion thereof, for use in the claimed composition of this invention, is a MASP-2 inhibitory antibody comprising a heavy chain variable region comprising 1) CDR-H1 comprising the amino acid sequence of 31-35 of SEQ ID NO: 2, 2) CDR-H2 comprising the amino acid sequence of 50-65 of SEQ ID NO: 2, 3) CDR-H3 comprising the amino acid sequence of 95-107 of SEQ ID NO: 2; and b) a light chain variable region comprising 1) CDR-L1 comprising the amino acid sequence of 24-34 of SEQ ID NO: 3, 2) CDR-L2 comprising the amino acid sequence of 50-56 of SEQ ID NO: 3, and 3) CDR-L3 comprising the amino acid sequence of 89-97 of SEQ ID NO: 3. In some embodiments, the MASP-2 inhibitory antibody, for use in the claimed composition of this invention, is a MASP-2 inhibitory antibody of the OMS646 variety having a heavy chain variable region with at least 95% similarity to SEQ ID NO: 2 and a light chain variable region with at least 95% similarity to SEQ ID NO: 3.In some embodiments, the MASP-2 inhibitory antibody, for use in the claimed combination of this invention, is a MASP-2 inhibitory antibody of the OMS646 variety that contains a mirror acid sequence with at least 95% similarity to SEQ ID NO:2, such that residue 31, R, residue 32, G, residue 33, K, residue 34, M, residue 35, G, residue 36, V, residue 37, S, residue 50, L, residue 51 A, residue 52, H, residue 53, I, residue 54, F, residue 55, S, residue 56, S, residue 57, D, residue 58, E, residue 59, a K, residue 60 a S, residue 61 Y, residue 62, R, residue 63 T, residue 64, S, residue 65 L, residue 66, K, residue 67 S, residue 95, Y, 96, Y, 97, C, 98, A, 99, R, 100, I, 101, R, 102, R or A, 103, G, 104, G, 105, I, 106, D, and 107, Y.and b) a light chain variable region comprising an amino acid sequence having at least 95% similarity to SEQ ID NO: 3, such that residue 23 is S, residue 24 is G, residue 25 is E or D, residue 26 is K, residue 27 is L, residue 28 is G, residue 29 is D, residue 30 is K, residue 31 is Y or F, residue 32 is A, residue 33 is Y, residue 49 is a Q, residue 50 is D, residue 51 is K or N, residue 52 is Q or K, residue 53 is R, residue 54 is P, residue 55 is S, residue 56 is G, residue 88 is Q, residue 89 is A, residue 90 is W, residue 91 is D, residue 92 is S, residue 93 is S, residue 94 is T, residue 95 is an A, residue 96 is V, and residue 97 is F. In some embodiments, the MASP-2 inhibitory antibody (e.g., OMS646 or a variant thereof), for use in the claimed composition of this invention, is a fully human monoclonal antibody. In some embodiments, the MASP-2 inhibitory monoclonal antibody is a fully human IgG4 antibody. In some embodiments, it comprises a point mutation in the hinge region to increase the stability of the antibody. In some embodiments, the MASP-2 inhibitory antibody (e.g., OMS646 or a variant thereof) comprises human variable regions linked to the IgG4 heavy chain and lambda light chain regions, such that the heavy chain comprises a point mutation in the hinge region (e.g., such that the IgG4 molecule comprises the S228P mutation) to increase antibody stability. In some embodiments, the MASP-2 inhibitory antibody is a tetramer comprising two identical heavy chains having the amino acid sequence of SEQ ID NO:4 and two identical light chains having the amino acid sequence of SEQ ID NO:5. In some embodiments, the concentration of MASP-2 inhibitory antibody in the composition is from about 100 mg / mL to 250 mg / mL, for example, from about 150 mg / mL to about 220 mg / mL, from 175 mg / mL to 200 mg / mL, or from about 175 mg / mL to about 195 mg / mL. In some embodiments, the concentration of MASP-2 inhibitory antibody in the composition is about 175 mg / mL to about 195 mg / mL, e.g., from about 180 mg / mL to about 190 mg / mL, from about 175 mg / mL, such as about 180 mg / mL, about 181 mg / mL, about 182 mg / mL, / about 183 mg / mL, about 184 mg / mL, about 185 mg / mL, / about 186 mg / mL, about 187 mg / mL, about 188 mg / mL, about 189 mg / mL or / about 190 mg / mL. In some embodiments, minor changes in the amino acid sequence of the MASP-2 inhibitory antibody or antigen-binding portion thereof are made in the claimed composition of the present invention, provided that the amino acid sequence changes retain at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similarity to the MASP-2 inhibitory antibodies or antigen-binding portion thereof (i.e., at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similarity to SEQ ID NO: 2 and / or at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similarity to SEQ ID NO: 3) and retain the ability to inhibit MASP-2-mediated antibody activation. It is understood that the MASP-2 inhibitory antibody or antigen-binding portion thereof referred to in the present disclosure can be produced using techniques known in the art (e.g., recombinant technologies, bacteriophage display technologies, synthetic technologies, or combinations thereof, or other technologies known in the art). Methods for producing and purifying antibodies or antigen-binding portions thereof are well known in the art and can be found, for example, in Harlow and Lane (1988) Antibodies, A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, Chapters 5-8 and 15. For example, a MASP-2 inhibitory antibody, such as OMS646, can be expressed in a suitable mammalian cell line. The sequences encoding the heavy chain variable region and the light chain variable region of a desired antibody, such as OMS646 (e.g., SEQ ID NO: 6 and SEQ ID NO: 7), can be used to transform a suitable mammalian host cell. Methods for introducing heterologous polynucleotides into mammalian cells are well known in the art and include techniques such as dextran-mediated transfection, calcium phosphate precipitation, polybrene-mediated transfection, protoplast fusion, electroporation, encapsulation of polynucleotides in liposomes, and direct microinjection of DNA into the nucleus. Existing mammalian cell lines are known to be hosts for expression in this context and include many immortalized cell lines available from the American Type Culture Collection (ATCC), and others include Chinese hamster ovary cells, HeLa cells, baby hamster kidney (BNK) cells, monkey kidney (COS) cells, human hepatocellular carcinoma cells (such as HepG2), human renal epithelial 293 cells (HEK293), and many other cell lines. Following the protein production phase of the cell culture process, the MASP-2 inhibitory antibody is recovered from the cell culture medium using methods known to those skilled in the art. In certain embodiments, the MASP-2 inhibitory antibody heavy and light chain polypeptides are recovered as secreted polypeptides from the culture medium. The MASP-2 inhibitory antibody can be purified, for example, by hydroxyapatite chromatography, gel electrophoresis, dialysis, and adsorption chromatography, or any method known or later learned, including protein A chromatography, ion-exchange column chromatography, ethanol precipitation, reverse-phase HPLC, silica chromatography, heparin SEPHAROSET® chromatography, anionic or cationic resin chromatography (such as a polyaspartic acid column), focusing chromatography, SDS-PAGE, and ammonium sulfate precipitation. The purification method can also include additional steps that remove or inactivate viruses and retroviruses that may be present in the mammalian cell line culture medium. A significant number of viral removal steps are available, including but not limited to treatment with chaotropes such as urea or guanidine, detergents, additional ultrafiltration / diafiltration steps, conventional separations, such as ion or size exchange chromatography, pH, heat, proteases, organic solvents, or any combination thereof. Purified MASP-2 inhibitor antibodies typically require concentration and buffer exchange prior to storage or further processing. For example, but not limited to, a tangential flow filtration (TFF) system may be used to concentrate and buffer exchange the previous purification column with the final buffer desired for the drug substance. The monoclonal MASP-2 inhibitory antibody described herein is substantially and preferably pure and more preferably homogeneous (i.e., free of contaminating proteins, etc.). By "substantially pure" antibody is meant a composition that is at least 90% by weight, based on the total weight of the composition, and preferably 95% by weight, composed of antibody. By "substantially homogeneous" antibody is meant a composition that is at least 99% by weight, based on the total weight of the composition, composed of antibody. Aqueous solution The low viscosity, high concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention comprises an aqueous solution containing a buffer system with a pH of 4.0 to 8.0 (e.g., a pH of about 5.0 to about 7.0 or a pH of about 5.5 to 6.5) and a MASP-2 inhibitory antibody (e.g., OMS646 or a variant thereof) or antigen-binding fragment thereof at a concentration of about 50 mg / mL to about 250 mg / mL (including about 100 mg / mL to 250 mg / mL). The aqueous solution for use in the compositions claimed in the present disclosure is one that is pharmaceutically acceptable (safe and non-toxic for injection into humans) and is useful for preparing the composition in liquid form. In some cases, the aqueous solution is water, such as sterile water for injection (WFI), which is a sterile, solute-free composition in the form of distilled water. It is also possible that other aqueous solutions that are suitable for therapeutic injection and do not adversely affect the stability of the composition, such as deionized water, can also be used.Other suitable aqueous solutions include bacteriostatic water for injection (BWFI), sterile saline solution, Ringer's solution, or other aqueous solutions used for pharmaceutical formulations. Buffering system The pH of the low viscosity, high concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is adjusted to 4.0 to 8.0, and preferably 5.0 to 7.0. The desired pH is suitably maintained using a buffer system. In some embodiments, the buffer system comprises at least one pharmaceutically acceptable buffering agent with a dissociation constant within 2 pH units of the pH of the composition. The buffer system used in the formulation according to the present invention has a pH in the range of about 4.0 to 8.0. Various types of buffers are known to those skilled in the art. Examples of buffering agents that control the pH in this range include acetate, succinate, gluconate, histidine, citrate and other organic acid buffers. In some embodiments, the buffering agent is selected from the group consisting of succinate, histidine and citrate. In some embodiments, the pharmaceutical compositions contain a buffer system with a buffering agent at a concentration of 1 to 50 mM, including 10 to 40 mM, or 10 to 30 mM, or 20 to 30 mM, or about 20 mM. In some embodiments, a "histidine buffer" is a buffer containing the amino acid histidine. Examples of histidine buffers include histidine or any of histidine salts including histidine hydrochloride, histidine acetate, histidine phosphate, and histidine sulfate, including combinations of any of these salts with or without histidine. In one embodiment, the buffer system comprises a histidine hydrochloride buffer (L-Histidine / HCL). Such a histidine hydrochloride buffer can be prepared by stabilizing L-histidine (unbased, solid) with dilute hydrochloric acid or by using a suitable combination of histidine and histidine hydrochloride. In some embodiments, the pH of the L-Histidine / HCl buffer is about 5.0 to 7.0, such as about 5.5 to 6.0, for example, about 5.8 or about 5.9. In some embodiments, the buffering agent is a citrate buffer. Such a citrate buffer may be prepared by titrating citric acid, the monosodium salt of citric acid and / or the disodium salt of citric acid with a dilute sodium hydroxide solution at an appropriate pH or by using a suitable mixture of citric acid and salt(s) to achieve the same pH. In another embodiment, a sodium citrate titration buffer may be prepared by titrating a solution of trisodium citrate with a dilute hydrochloric acid solution to an appropriate pH. In this case, the ionic strength may be slightly higher than the initial ionic strength of the citric acid, due to the production of excess sodium and chloride ions in the solution. In certain embodiments, the pH of the citrate buffer is from about 5.0 to about 7.0, such as from about 5.5 to 6.0, for example, about 5.8 or about 5.9. In some embodiments, the buffering agent is a succinate buffer. In certain embodiments, the pH of the succinate buffer is about 5.5 to 6.0, for example about 5.8 or 5.9. In some embodiments, the buffering agent is a sodium citrate buffer such that the concentration of sodium citrate present in the composition is about 10 to 50 mM, including 10 to 25 mM, such as about 20 mM. In some embodiments, the buffering agent is an L-histidine buffer such that the concentration of L-histidine present in the composition is about 10 to 50 mM, including 10 to 25 mM, such as about 20 mM. In some embodiments, the composition comprises about 20 mM sodium citrate and has a pH of about 5.0 to 7.0. In some embodiments, the composition comprises about 20 mM L-histidine and has a pH of about 5.0 to 7.0. Additive In some embodiments, the low viscosity, high concentration MASP-2 inhibitory antibody pharmaceutical composition of the present invention further comprises an additive. Examples of suitable additives include proteins (e.g., serum albumin), amino acids (e.g., aspartic acid, glutamic acid, lysine, arginine, glycine, and histidine), saccharides (e.g., glucose, sucrose, maltose, and trehalose), polyols (e.g., mannitol and sorbitol), fatty acids, and phospholipids (e.g., alkyl sulfonates and caprylate). In some embodiments, the composition comprises an additive selected from the group consisting of an amino acid with a charged side chain, another sugar or polyol, and a salt. In some embodiments, the composition comprises another sugar or polyol, such as sucrose, trehalose, mannitol, or sorbitol. In some embodiments, the composition comprises a salt, such as NaCl or a salt of an amino acid. In some embodiments, the formulation contains an additive that is a tonicity modifying agent. In some embodiments, the tonicity modifying agent is present in the composition at a concentration suitable for providing an isotonic composition. In some embodiments, the tonicity modifying agent is present in the composition at a concentration suitable for providing a hypertonic composition. In some embodiments, the tonicity modifying agent is from the group of an amino acid with a charged side chain, another sugar or polyol, and a salt. In some embodiments, the tonicity modifying agent is an amino acid with a charged side chain (i.e., a negatively charged side chain or a positively charged side chain) at a concentration of about 50 mM to 300 mM. In some embodiments, the tonicity modifying agent is an amino acid with a negatively charged side chain, such as glutamate. In some embodiments, the composition contains glutamate at a concentration of about 50 mM to 300 mM. In some embodiments, the tonicity modifying agent is an amino acid with a positively charged side chain, such as arginine.In some embodiments, the composition comprises arginine (e.g., arginine HCL) at a concentration of about 50 mM to 300 mM, such as about 150 mM to 225 mM. Preferably, the pharmaceutical compositions disclosed herein are hypertonic (i.e., have an osmotic pressure higher than that of human blood). As described herein, it was unexpectedly observed in studies that hypertonicity, achieved by slightly increasing the concentration of arginine, caused a decrease in the viscosity of the sample. As described in Example 2, it was unexpectedly observed in studies that low viscosity (e.g., less than 25 cP) was achieved with MASP-2 inhibitory antibody compositions at high citrate / arginine and histidine / arginine concentrations, where the arginine concentration was 200 or greater in the absence of CaCl2. Similarly, in some embodiments, the composition comprises arginine (e.g., arginine HCL) at a hypertonic concentration of about 200 mM to 300 mM. As described in Example 2, it was observed that compositions containing divalent cations (CaCl2 or MgCl2) had higher molecular weight materials compared to compositions without CaCl2 or MgCl2 additives. Similarly, in one embodiment, the low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is substantially free of CaCl2 additives. In one embodiment, the low viscosity, high concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is substantially free of MgCl2 additives. As described in Example 2, for the high concentration MASP-2 inhibitory antibody pharmaceutical composition, it was found that the addition of sucrose was associated with increased polydispersity in all buffer systems tested. Similarly, in one embodiment, the low viscosity, high concentration MASP-2 inhibitory antibody of the present invention is sucrose-free. As described in Example 2, for the high concentration MASP-2 inhibitory antibody pharmaceutical composition, the addition of sorbitol was found to be associated with increased polydispersity in all buffer systems tested. Similarly, in one embodiment, the low viscosity, high concentration MASP-2 inhibitory antibody of the present invention is free of sorbitol. Surfactant In some embodiments, optionally, the high-concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention also comprises a pharmaceutically acceptable surfactant. Examples of pharmaceutically acceptable surfactants include: polyoxyethylene sorbitan fatty acid esters (e.g., Tween), polyethylene-polypropylene glycols, polyoxyethylene-stearates, polyoxyethylene alkyl ethers (e.g., polyoxyethylene monolauryl ether), alkylphenylpolyoxyethylene ethers (e.g., Triton-X), polyoxyethylene-polyoxypropylene copolymers (e.g., Poloxamer and Pluronic), and sodium dodecyl sulphate (SDS). In some embodiments, the high-concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention comprises a non-ionic surfactant. The non-ionic surfactant can be a polysorbate (e.g., selected from the group consisting of polysorbate 20, polysorbate 80, and polyethylene-polypropylene copolymer). In some embodiments, the surfactant concentration is about 0.001 to 0.1% (w / v), or 0.005% to 0.1% (w / v), or 0.01 to 0.1% (w / v), or 0.01 to 0.08% (w / v), or 0.025 to 0.075% (w / v) or more particularly about 0.01% (w / v), about 0.02% (w / v), about 0.04% (w / v), or about 0.06% (w / v), or about 0.08% (w / v) or about 10% (w / v). In some embodiments, the composition comprises a nonionic surfactant (e.g., polysorbate 80) at a concentration of 0.001 to 0.1% (w / v), or 0.005% to 0.1% (w / v), or 0.01 to 0.1% (w / v), or 0.01 to 0.08% (w / v), or 0.025 to 0.075% (w / v), or particularly about 0.01% (w / v), about 0.02% (w / v), about 0.04% (w / v), or about 0.06% (w / v), or about 0.08% (w / v), or about 10% (w / v). As described in Example 2, the researchers unexpectedly observed that the addition of the non-ionic surfactant polysorbate 80 (PS-80) resulted in a further reduction in viscosity while also protecting protein recovery, thereby providing a high concentration of the OMS646 antibody while also providing a low viscosity suitable for use in injection devices such as auto-injectors. Stabilizers In some embodiments, the high concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention also includes a stabilizer. The stabilizer (which is used synonymously with "stabilizing agent" herein) may be a carbohydrate or saccharide or a sugar, for example, trehalose or sucrose, which is approved as an additive in pharmaceutical compositions by the authorities. The typical concentration of the stabilizer is 15 to 250 mM, or 150 to 250 mM, or about 210 mM. The composition may contain a secondary stabilizer such as methionine, which is used, for example, at a concentration of 5 to 25 mM or at a concentration of 5 to 15 mM (e.g., methionine at a concentration of about 5 mM, about 10 mM, or about 15 mM). Holders In some embodiments, optionally, the high-concentration MASP-2 inhibitory antibody pharmaceutical composition according to the present invention also includes a preservative (e.g., antimicrobial agent). Antimicrobial agents are generally required for injectable products that are intended for multiple doses. Similarly, if the active ingredient does not have antibacterial or bacteriostatic properties, or if it promotes bacterial growth, preservatives are added to pharmaceutical compositions that are formulated in vials for single doses. Some common preservatives include: benzyl alcohol (0.9% to 1.5%), methylparaben (0.18% to 0.2%), propylparaben (0.02%), benzalkonium chloride (0.01% to 0.02%), and trimethoprim (0.001% to 0.01%). Syringe tolerance The subcutaneous route of administration requires the use of an injection device, such as a syringe, auto-injector, injection pump, or other device. This limits the product formulation with respect to the volume of injection and the viscosity of the solution. In addition, the product formulation must be suitable for use in the injection device with respect to the force and time required for injection. The term “syringability,” as used herein, refers to the ability of an injectable drug to easily pass through a subcutaneous needle and into the reservoir of a syringe prior to injection. The term “injectability,” as used herein, refers to the performance of a composition during injection (Cilurzo F, Selmin F, Minghetti P, et al. Injectability Evaluation: An Open Issue. AAPS PharmSciTech. 2011;12(2):604-609). Syringability includes factors such as ease of withdrawal, clotting, and foaming tendency, and accuracy of dose measurements. Injectability includes the pressure or force required for injection, uniformity of flow, and lack of clogging (i.e., no blockage of the syringe needle).Syringability and injectability can be affected by needle geometry, e.g., internal diameter, length, outlet valve shape, and syringe end surface, especially in automated injection devices such as auto-injectors (equipped with 29–31 GA needles) and prefilled syringes (equipped with 24–27 GA needles). Injection force (or draw force) is a complex factor that is influenced by solution viscosity, needle size (e.g., gauge needle), and container / package surface tension. Smaller needles, e.g., ≥ gauge needle, will cause less pain in patients. Overcashier et al. defined the relationship between viscosity and draw force as a function of gauge needle in the Hagen-Poisson equation (Overcashier et al., Am Pharm Rev 9(6):77–83 (2006)). For example, with a thin-walled needle, with a gauge of 27, the viscosity of the liquid must be kept below 20 cP so that the injection force does not exceed 25 newtons (N). In some embodiments, the pharmaceutical composition of the present invention, when injected through a 27 gauge (1.25”) needle at room temperature, has an injection force of about 25 N or less. In some embodiments, the pharmaceutical composition of the present invention, when injected through a 25 gauge (1”) needle at room temperature, has an injection force of about 20 N or less. As shown in Example 3, the high-concentration, low-viscosity MASP-2 inhibitory antibody pharmaceutical composition of the present invention (e.g., OMS646) has excellent injectability and syringability. The low-viscosity MASP-2 inhibitory antibody pharmaceutical composition of the present invention allows for intramuscular or subcutaneous injection through small needles, e.g., 27 GA (1.25”), 25GA (1”), and 25GA thin-walled (1”). In some cases, the low viscosity of the MASP-2 inhibitory antibody pharmaceutical composition of the present invention allows for injection of a tolerable amount (e.g., 1-3 cc) and delivery of an effective amount of MASP-2 inhibitory antibody in a single injection at a single injection site. Sustainability For each of the above, it should be noted that the MASP-2 inhibitory antibody or antigen-binding portion thereof should retain the ability to inhibit MASP-2-mediated activation of the helper antibody. For example, as described in Example 1 or other methods of inhibiting the lectin pathway, for example in WO2012 / 151481, the MASP-2 inhibitory antibody retains the ability to bind to MASP-2 and inhibit lectin pathway activity. In addition to potency tests, various physical and chemical tests can be used to assess stability, including isoelectric focusing, polyacrylamide gel electrophoresis, chromatographic measurements, and evaluation of primary and secondary visible particles. In some embodiments, as described in the stability studies in Examples 2 and 4, the composition of the present invention is stable at a temperature range of -20°C to 8°C for at least 30 days, at least 9 months or more, or at least 12 months or more. In addition, in some embodiments, the compositions are stable at a temperature range of -20°C to 8°C, including 2°C to 8°C, for at least 6 months, at least 1 year, or at least 2 years or more. In some embodiments, stability may be assessed, for example, by maintaining a level of purity over time. For example, in some cases, it has been determined by size-free chromatography (SEC) that measures the presence or absence of dissociated (LMW) and / or aggregated (HMW) species that the compounds of the present disclosure exhibit less than 5%, such as less than 4%, such as less than 3%, such as less than 2%, such as less than 1%, purity loss per month, 6 months, 9 months, or 1 year at 2 to 8°C. In some embodiments, the compounds of the present disclosure exhibit zero or very little degradation or aggregation, and the compounds retain their properties after storage for specified periods of time. In other words, the formulations herein are capable of maintaining the structural integrity of the MASP-2 inhibitory antibody OMS646 at high concentrations in solution, e.g., greater than 150 mg / mL, or greater than 175 mg / mL, or at least 185 mg / mL, such that the MASP-2 inhibitory antibody can remain substantially monomeric (e.g., at least 95% or greater) after storage for specified periods of time at a temperature of about 2 to 8°C. Preferably, after storage for the specified period at a temperature of about 2 to 8°C, in size-free chromatography (SEC) analysis, less than 5%, less than 4%, less than 3%, less than 2%, less than 1% and most preferably less than 0.5% of the antibody should be in the dissociated (LMW) or aggregated (HMW) form. As described in Example 4 herein, the inventors provide compositions suitable for maintaining about 185 mg / mL of the MASP-2 inhibitory antibody, namely OMS646, in the monomeric state for at least 12 months at about 2 to 8°C. Tissue permeability modifier In another embodiment of the invention, the high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention comprises a tissue permeability modifier that enhances the absorption or dispersion of the MASP-2 inhibitory antibody after injection (e.g., subcutaneous injection). In some embodiments, the tissue permeability modifier is a hyaluronidase enzyme that functions as a tissue permeability modifier and enhances the dispersion and absorption of the injected MASP-2 inhibitory antibody. One particular tissue permeability modifier is hyaluronidase (e.g., a recombinant human hyaluronidase). Hyaluronidase acts as a tissue permeability modifier by temporarily breaking down the hyaluronan barrier and allowing access to lymphatic and capillary vessels, allowing for rapid absorption of the injected material into the circulatory system. Hyaluronan is naturally regenerated and the barrier is fully regenerated, e.g., within 48 hours.The addition of hyaluronidase to the injectable formulation increases the bioavailability of the MASP-2 inhibitor antibody after injection, especially subcutaneous injection. It also allows for a larger injection site volume (i.e., greater than 1 mL) with less pain and discomfort, and minimizes the incidence of injection site reactions (e.g., injection site loosening). In some embodiments, the high-concentration, low-viscosity MASP-2 inhibitory antibody pharmaceutical composition of the present invention comprises about 100 U / mL to about 20,000 U / mL of hyaluronidase enzyme. The actual concentration of hyaluronidase enzyme depends on the type of hyaluronidase enzyme used in preparing the MASP-2 inhibitory antibody of the present invention. An effective amount of hyaluronidase can be determined by one skilled in the art. The amount should be adjusted to enhance the dispersion and absorption of the MASP-2 inhibitory antibody injected simultaneously or sequentially. The minimum amount of hyaluronidase enzyme is greater than 100 U / mL. More specifically, the effective amount of the hyaluronidase enzyme is from about 150U / ml to about 20,000 U / ml, such that said amount corresponds to about 0.01 to 0.16 mg of protein based on a hypothetical activity of 100,000 U / mg. In some embodiments, the pharmaceutical compositions contain hyaluronidase at a concentration of 1,000 to 20,000 U / ml, including 1,000 to 16,000 U / ml.It is also possible that the concentration of hyaluronidase is about 1500 to 12000 U / mL or from 2000 U / mL to about 12000 U / mL. The values ​​specified herein correspond to the amount of hyaluronidase initially added to the pharmaceutical composition. In some embodiments of the invention, the ratio (w / w) of hyaluronidase to MASP-2 inhibitory antibody is in the range of 1:1,000 to 1:8,000 or in the range of 1:4,000 to 1:6,000 or in the range of about 1:4,000 to 1:5,000. Hyaluronidase can be present as a component of a high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention or it may be provided as a separate solution in a therapeutic kit. Thus, in one embodiment, the MASP-2 inhibitory antibody is combined with hyaluronidase. In another embodiment, the MASP-2 inhibitory antibody and hyaluronidase are formulated separately and mixed prior to subcutaneous injection. In another embodiment, the MASP-2 inhibitory antibody and hyaluronidase are each formulated separately and injected, e.g., the hyaluronidase is injected as a separate injection directly before or after the injection of the formulation containing the MASP-2 inhibitory antibody. In some embodiments, the hyaluronidase is injected subcutaneously from about 5 seconds to about 30 minutes prior to the injection of the pharmaceutical composition containing the MASP-2 inhibitory antibody, at the same injection site.In some cases, the MASP-2 inhibitory antibody drug combination and the hyaluronidase solution are placed in separate channels of the injection device and are injected either simultaneously or sequentially. Pre-filled injection devices In another aspect of the present invention, a high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is placed in a pre-filled sealed container in an amount suitable for injection into a mammal. Thus, a sufficient amount of the pharmaceutical composition prepared in accordance with the present disclosure, which is equal to or only slightly more than the amount of MASP-2 inhibitory antibody desired for a mammalian subject (i.e., no more than a 25% excess, such as no more than a 10% excess), is placed in a pre-filled container, which facilitates the release of the antibody composition upon injection. In some embodiments, the pre-filled container contains at least one unit of MASP-2 inhibitory antibody. For example, the desired amount for a single dose of a low viscosity MASP-2 inhibitory antibody drug can be contained in a prefilled package such as a stoppered glass vial or other container from which a needle can be withdrawn, or it can be contained in a syringe or other suitable means for injection. Examples of such containers include vials, syringes, ampoules, bottles, cartridges, and bags. The composition is preferably contained in disposable prefilled syringes made of glass or polymeric materials such as cyclic olefin polymers or styrene butadiene acrylonitrile (ABS), polycarbonate (PC), polyoxymethylene (POM), polystyrene (PS), polyethylene terephthalate (PBT), polypropylene (PP), polyethylene (PE), polyamide (PA), thermoplastic elastomer (TPE), or a combination thereof. The reservoir of these syringes is operated by an elastomeric piston, which can move along the reservoir to deliver the liquid contents to the injection site through a needle attached to the reservoir. In some embodiments of the present invention, each syringe includes a needle attached thereto. In some embodiments, the high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is contained in a prefilled container selected from the following: a syringe (e.g., a single or dual bore syringe), a pen ampoule, a sealed vial (e.g., a dual vial), an auto-injector, an injection pump device (e.g., a body patch pump, a connected pump, or an osmotic pump). For subcutaneous delivery, the composition may be contained in a prefilled device such as a prefilled syringe, an auto-injector, an injection device (e.g., an INJECT-EASE™ or GENJECT™ device), a pen syringe (e.g., a GENPENT™), or other device suitable for subcutaneous injection. The composition of the present disclosure can be provided as a unit dose composition in a prefilled container, suitable for self-administration by the patient. For example, a unit dose per vial, cartridge, or other prefilled container (e.g., disposable syringe or pen) can be about 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, 1.1 mL, 1.2 mL, 1.3 mL, 1.4 mL, 1.5 mL, 1.6 mL, 1.7 mL, 1.8 mL, 1.9 mL, 2.0 mL, 2.1 mL, 2.2 mL, 2.3 mL, 2.4 mL, 2.5 mL, 2.6 mL, 2.7 mL, 2.8 mL, 2.9 mL, 3.0 mL. liters, 3.5 ml, 4.0 ml, 4.5 ml, 5.0 ml, 5.5 ml, 6.0 ml, 6.5 ml, 7.0 ml, 7.5 ml, 8.0 ml, 8.5 ml, 9.0 ml, 9.5 ml or about 10.0 mL or more of a high concentration MASP-2 inhibitory antibody pharmaceutical composition (e.g., OMS646) in the range of about 100 mg / mL to about 250 mg / mL, about 150 mg / mL to about 200 mg / mL, about 175 mg / mL to about 200 mg / mL, such as about 185 mg / mL, resulting in a unit dose of about 20 mg to about 1000 mg or more per container. In some embodiments, the composition of the present disclosure can be provided as a unit dosage composition in a prefilled container, e.g., a vial or syringe, in dosages of about 350 mg to 400 mg, such as about 350 mg, about 360 mg, about 370 mg, about 380 mg, about 390 mg, or about 400 mg. In some embodiments, the present disclosure composition can be provided as a unit dose composition in a prefilled container having a volume of 0.1 mL to 3.0 mL, such as 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, 1.1 mL, 1.2 mL, 1.3 mL, 1.4 mL, 1.5 mL, 1.6 mL, 1.7 mL, 1.8 mL, 1.9 mL, 2.0 mL, 2.1 mL, 2.2 mL, 2.3 mL, 2.4 mL, 2.5 mL, 2.6 mL, 2.7 mL, 2.8 mL, 2.9 mL, or thereabouts. 3.0 ml containing about 20 to 750 mg of MASP-2 inhibitory antibody (e.g. OMS646). As described herein, stable compositions prepared in unit dosage form can be administered directly (e.g., via subcutaneous injection) to a subject or prepared in a manner that requires dilution prior to administration to a patient. The composition of the present disclosure can be sterilized by various sterilization methods suitable for antibody compositions, such as sterile filtration. In some embodiments, the antibody composition is sterilized, for example, with a pre-sterilized 0.2 micron filter. The sterilized compositions of the present disclosure can be administered to a subject to prevent, treat, or ameliorate a disease or disorder resulting from MASP-2-mediated antibody activation. In another aspect, a method of making a device for filling a container with a high concentration of a MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is provided. In one embodiment of the present invention, the present disclosure provides a pharmaceutical composition for treating a patient suffering from or at risk of developing a MASP-2-mediated disease, wherein the composition comprises a sterile, single-use dosage form containing about 350 mg to 400 mg (i.e., 350 mg, 360 mg, 370 mg, 380 mg, 390 mg, or 400 mg) of a MASP-2 inhibitory antibody, wherein the composition comprises about 1.8 mL to about 2.2 mL (i.e., 1.8 mL, 1.9 mL, 2.0 mL, 2.1 mL, or 2.2 mL) of a 185 mg / mL antibody composition, wherein the antibody or fragments thereof comprise a) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and b) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2. It is an amino acid used as SEQ ID NO:3, such that the compound remains stable after at least six months of storage at a temperature between 2 and 8 degrees Celsius.In some embodiments, the MASP-2-induced disease is selected from the group consisting of: aHUS, HSCT-TMA, lupus nephritis (LN), and IgAN. Kits containing MASP-2 inhibitory antibody drug combination with high concentration and low viscosity The present disclosure also includes therapeutic kits comprising at least one container containing a high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition. In some embodiments, the present invention includes a kit comprising a) a container containing any MASP-2 inhibitory antibody composition described herein and b) a device suitable for delivering the composition to a patient in need thereof. In some embodiments of any of the kits described herein, said device is suitable for subcutaneous delivery of the composition to the patient. Various types of containers are suitable for containing the MASP-2 inhibitory antibody pharmaceutical compositions included in the kits of the present invention. In some embodiments of the kits of the present invention, the container is a prefilled syringe (e.g., a single-needle or double-needle) or a sealed prefilled vial. In some embodiments, the container containing the high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention is selected from the following: a syringe (e.g., a single or double bore syringe), a pen ampoule, a sealed vial (e.g., a double bore vial), an auto-injector, an injection pump device (e.g., a body patch pump, a connected pump, or an osmotic pump). For subcutaneous delivery, the composition may be contained in a pre-filled device, such as a pre-filled syringe, an auto-injector, an injection device (e.g., an INJECT-EASE™ or GENJECT™ device), a pen syringe (e.g., a GENPENT™), or other device suitable for subcutaneous injection. In addition to the containers filled with a single dose of the pharmaceutical composition, the kit of the present invention can also include an outer container containing the pre-filled container. For example, the outer container may be a plastic or cardboard tray having recesses in which the pre-filled container is placed and which holds it stationary during transportation and prior to use. In some embodiments, the outer container is opaque and serves to protect the pre-filled container from light, preventing light-induced degradation. For example, the plastic or cardboard tray in which the pre-filled container is placed can be packaged within a light-blocking paper carton. The kit of the present invention can also include a set of instructions for administering and using the MASP-2 inhibitory antibody composition according to the present invention, which may be printed on the outer container or on a sheet of paper that is placed in the outer container. In some embodiments, the kit includes a second container (e.g., a prefilled syringe) containing an effective dose of hyaluronidase. The kit may also include other items that are commercially and functionally appropriate, including needles, syringes, packaging, etc. Sample compositions As described above, the stable pharmaceutical composition of MASP-2 inhibitory antibody with high concentration and low viscosity according to the present invention comprises MASP-2 inhibitory antibody with a concentration of 50 mg / ml to 250 mg / ml in an aqueous solution containing a buffering agent with a pH of 4.0 to 8.0. The buffer system, such as histidine, citrate or succinate, is preferably used at about 10 to 50 mM, and preferably at about 20 mM. In some preferred embodiments, the composition also comprises an amino acid with a negatively charged side chain at a concentration of 50 to 300 mM. In some preferred embodiments, the composition also comprises an amino acid with a positively charged side chain, such as arginine, at a concentration of about 50 mM to 300 mM. In some preferred embodiments, the composition comprises a nonionic surfactant, such as polysorbate 80, at a concentration of 0.001 to 0.1% (w / v), such as 0.05% (w / v) to about 0.1% (w / v). In some embodiments, the composition comprises an enzyme, hyaluronidase, in an amount effective to enhance the dispersion and absorption of the MASP-2 inhibitory antibody administered to the patient. In some embodiments, the high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention comprises, consists of, or consists essentially of one of the following: a) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM histidine buffer at a pH of about 5 to 7; 100 mM to 225 mM arginine; and optionally 100 to 20,000 U / mL hyaluronidase. b) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM histidine buffer at a pH of about 5 to 7; 100 mM to 225 mM arginine; about 0.01% to 0.08% (w / v) nonionic surfactant; and optionally 100 to 20,000 U / mL hyaluronidase. c) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM citrate buffer with a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine and optionally 100 to 20,000 U / mL hyaluronidase. d) 100 to 200 mg / mL of MASP-2 inhibitory antibody; 10 to 50 mM citrate buffer with a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, about 0.01% to 0.08% (w / v) non-ionic surfactant; and optionally 100 to 20,000 U / mL of hyaluronidase. e) 100 to 200 mg / mL MASP-2 inhibitory antibody; 10 to 50 mM succinate buffer with a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine and optionally 100 to 20,000 U / mL hyaluronidase. c) 100 to 200 mg / mL of MASP-2 inhibitory antibody; 10 to 50 mM succinate buffer with a pH of about 5.0 to about 7.0; 100 mM to 225 mM arginine, about 0.01% to 0.08% (w / v) non-ionic surfactant; and optionally 100 to 20,000 U / mL of hyaluronidase. In some embodiments, the stable pharmaceutical composition of a high concentration, low viscosity MASP-2 inhibitory antibody according to the present invention comprises, consists of, or consists essentially of one of the following: g) 185+18.5 mg / mL MASP-2 inhibitor antibody; 20 ± 2 mM citrate buffer with pH approximately 5.8; 200 ± 20 mM arginine and optionally 100 to 20,000 U / mL of hyaluronidase. h) 185 + 18.5 mg / mL MASP-2 inhibitory antibody; 20 ± 2 mM citrate buffer with a pH of about 5.8; 200 ± 20 mM arginine, about 0.01% (w / v) polysorbate 80 and optionally 100 to 20,000 U / mL hyaluronidase. x) 185 + 18.5 mg / mL MASP-2 inhibitor antibody; 20 ± 2 mM histidine buffer with pH approximately 5.9, 200 ± 20 mM arginine and optionally 100 to 20,000 U / mL hyaluronidase. d) 185 + 18.5 mg / mL MASP-2 inhibitory antibody; 20 ± 2 mM histidine buffer at pH approximately 5.9, 200 ± 20 mM arginine, approximately 0.01% polysorbate 80 and optionally 100 to 20,000 U / mL hyaluronidase. Method for producing a pharmaceutical composition of MASP-2 inhibitory antibody with high concentration and low viscosity In another aspect, the present disclosure provides a method for producing a formulation comprising 100 mg / mL or more of a MASP-2 inhibitory antibody, the method comprising the steps of: a) preparing a primary pharmaceutical composition comprising purified OMS646, such that the primary pharmaceutical composition contains less than 50 mg / mL of OMS646 protein; b) subjecting the primary pharmaceutical composition to filtration to produce a secondary pharmaceutical composition, such that the secondary pharmaceutical composition has a different, secondary composition upon filtration; and c) concentrating the secondary pharmaceutical composition to produce a concentrated antibody solution containing 100 mg / mL or more of OMS646. The prepared solid solution is typically adjusted to a constant protein concentration so that the desired filling volume can be maintained constant. The liquid drug manufacturing process typically involves mixing the MASP-2 inhibitor antibody with a buffer system, additives, and optionally a surfactant, followed by sterilization and filling of vials (or other containers such as syringes) and sealing of the containers (capping, etc.). Table 1: Composition of sample 1 Elements added to water for injection OMS646 antibody concentration 185 mg / mL Sodium citrate 20 mM L-arginine HCL 200 mM Polysorbate 80 0.01% Table 2: Composition of sample 2 Elements added to water for injection OMS646 antibody concentration 185 mg / mL L-histidine 20 mM L-arginine HCL 200 mM Polysorbate 80 0.01% Treatment methods In another aspect, the present disclosure provides a method for treating a patient suffering from or at risk of developing a MASP-2-mediated disease comprising administering a high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition (such as OMS646) as described herein. As set forth in patent applications Nos. 7,919,094, 8,840,893, 8,652,477, 8,951,522, 9,011,860, 9,644,035, and patent publications Nos. US2013 / 0344073, US2013 / 0266560, US 2015 / 0166675, US2017 / 0137537, US2017 / 0189525, and pending applications Nos. 15 / 476,154, 15 / 347,434, 15 / 470,647, 62 / 315,857, 62 / 275,025, and 62 / 527,926 (all owned by Omeros Corporation) are), MASP-2-mediated activation of the helper antibody has been shown to contribute to the pathogenesis of many acute and chronic diseases. For example, as described in Patent No. 8,951,522, the primary function of the helper antibody system, part of the innate immune system, is to protect the host against infectious agents. However, inappropriate or excessive activation of the helper antibody system can lead to serious diseases such as thrombotic microangiopathy (TMAs, including aHUS, TTP, and HUS), which result in endothelial injury and fibrin- and platelet-containing thrombosis within the vessels, leading to serious damage to internal organs.The lectin pathway plays an important role in the activation of helper antibodies as a result of endothelial cell stress or injury, and preventing the activation of MASP-2 and the lectin pathway stops a series of enzymatic reactions that lead to the formation of the membrane attack complex, platelet activation, and leukocyte recruitment. As stated in patent number 8,652,477, in addition to initiating the lectin pathway, MASP-2 can also activate the coagulation system and is also capable of degrading prothrombin to thrombin. As described in Example 1 and Patent No. 9,011,860, OMS646 is a potent inhibitor of lectin-dependent antibody activation. This antibody does not show significant binding (at least 5000-fold lower affinity) to serine proteases of other antibody pathways, namely C1r, C1s, MASP-1, and MASP-3, and does not inhibit classical pathway-dependent antibody activation. Similarly, in some embodiments, the method comprises administering to a patient suffering from or at risk of developing a disease caused by a MASP-2-dependent antibody, an amount of a high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition according to the present invention, in an amount sufficient to inhibit the activation of the MASP-2-dependent antibody in the mammalian subject, thereby treating the disease. In some embodiments, the methods can be performed using any of the kits or prefilled containers (e.g., prefilled syringes or vials) described herein. . In some embodiments, the method can include determining, prior to administering the composition to the patient, whether the patient has a disease or disorder associated with a lectin antibody. In some cases, the method also includes injection of a tissue permeability modifier (e.g., hyaluronidase), which enhances the uptake or dispersion of the MASP-2 inhibitory antibody after injection.The tissue permeability modifier can be injected simultaneously with the MASP-2 inhibitory antibody formulation or sequentially (e.g., within 5 minutes of injection of the MASP-2 inhibitory antibody formulation at or near the injection site). In some embodiments, the method comprises injecting a primary prefilled syringe containing a high concentration, low viscosity MASP-2 inhibitory antibody pharmaceutical composition (e.g., OMS646) into a subject in need thereof to inhibit MASP-2-mediated antibody activation. In some embodiments, the method comprises injecting a secondary prefilled syringe containing a tissue permeability modifier such that the injection site is at or near the site of injection of the MASP-2 inhibitory antibody. In some cases, MASP-2-related antibody-induced diseases include: thrombotic microangiopathy (TMA) including thrombotic thrombocytopenic purpura (TTP), refractory TTP, Upshaw-Shulman syndrome (USS), Orlick hemolytic syndrome (HUS), atypical hemolytic syndrome (aHUS), atypical non-factor H-dependent hemolytic syndrome, aHUS due to infection, cancer-induced TMA, chemotherapy-induced TMA, organ transplant-induced TMA, or hematopoietic stem cell transplant-induced TMA. In some cases, MASP-2-related antibody-mediated diseases are intestinal diseases, examples of which include: mesangioproliferative glomerulonephritis, membranous glomerulonephritis, membranoproliferative glomerulonephritis (mesangiocapillary glomerulonephritis), acute post-infectious glomerulonephritis (post-streptococcal glomerulonephritis), C3 glomerulopathy, cryoglobulinemic glomerulonephritis, post-immune crescentic necrotizing glomerulonephritis, lupus nephritis, Henoch-Schoen purpura nephritis, and IgA nephropathy. In some embodiments, the MASP-2 antibody-related disease is intestinal fibrosis (e.g., tubulointerstitial fibrosis) and / or proteinuria in a subject with or at risk for chronic kidney disease, chronic renal failure, glomerular disease (e.g., central segment glomerulosclerosis), immune-mediated disorders (e.g., IgA nephropathy, membranous nephropathy), lupus nephritis, nephrotic syndrome, diabetic nephropathy, tubulointerstitial cell damage and glomerulonephritis (e.g., C3 glomerulopathy) or a disease associated with proteinuria including nephrotic syndrome, preeclampsia, eclampsia, toxic kidney lesions, amyloidosis, collagen vascular diseases (e.g., systemic lupus erythematosus), dehydration, glomerular diseases (e.g., membranous glomerulonephritis, central segment glomerulonephritis, C3 glomerulopathy, scleroderma partial, lipoid nephrosis) intense exercise, stress, arthritis, proteinuria (pastoral), central segment glomerulosclerosis, IgA nephropathy (eg, Berger's disease), IgM nephropathy, membranoproliferative glomerulonephritis, membranous nephropathy, partial change disease, sarcoidosis, Alport syndrome,Type 1 diabetes (diabetic nephropathy), drug intoxication (e.g., NSAIDS, nicotine, penicillamine, lithium carbonate, gold and other heavy metals, ACE inhibitors, antibiotics (e.g., adriamycin) or opiates (e.g., heroin) or other nephrotoxins), Fabry disease, infections (e.g., HIV, syphilis, hepatitis A, B, or C, post-streptococcal infection, urinary schistosomiasis), aminoaciduria, Fankeni syndrome, hypertensive nephrosclerosis, interstitial nephritis, sickle cell disease, hemoglobinuria, multiple myeloma, myoglobinuria, transplant rejection (e.g., kidney transplant rejection), Ebola hemorrhagic fever, Neelpatella syndrome, Familial Mediterranean fever, HELLP syndrome, systemic lupus erythematosus, Wegener's granulomatosis, glycogen storage rheumatoid arthritis type 1, Goodpasture syndrome, Henoch-Schoen purpura, urinary tract infection Urine that has spread to the kidneys is Sjögren's syndrome and post-infectious glomerulonephritis. In some cases, MASP-2-related autoimmune disease is an inflammatory reaction resulting from a tissue or whole organ transplant, including allotransplantation or xenotransplantation of a whole organ (e.g., kidney, heart, liver, pancreas, lung, cornea, etc.) or tissue transplant (e.g., valves, tendons, bone marrow, etc.). In some instances, the MASP-2-related antibody-induced disease is an ischemia reperfusion (I / R) injury, including cardiac I / R, gastrointestinal I / R, renal I / R, I / R following aortic aneurysm repair, I / R resulting from cardiopulmonary bypass, cerebral I / R, stroke, organ transplantation or retransplantation of amputated and damaged organs or members, revascularization to a transplant or retransplantation, and hemodynamic restoration following shock and / or surgery. In some cases, the MASP-2-related autoimmune disease is a non-obesity diabetes (type 1 diabetes or insulin-dependent gestational diabetes) and / or a type 1 or 2 (adult-onset) diabetes complex including diabetic angiopathy, diabetic neuropathy, diabetic retinopathy, or diabetic macular edema. In some cases, MASP-2-related antibody disease is a cardiovascular disease or disorder, including Henoch-Schoen purpura nephritis, systemic lupus erythematosus vasculitis, rheumatoid arthritis vasculitis (also known as malignant rheumatoid arthritis), immune-mediated vasculitis and Takayasu disease, dilated cardiomyopathy, diabetic angiopathy; Kawasaki disease (arthritis); venous gas embolism (VGE); and inhalational inhibition following stent placement, bypass atherectomy, and / or percutaneous transluminal coronary angioplasty (PTCA). In some cases, MASP-2-related autoimmune disease is an inflammatory gastrointestinal disorder, including pancreatitis, diverticulitis, and intestinal disorders including Crohn's disease, ulcerative colitis, irritable bowel syndrome, and inflammatory bowel disease (IBD). In some cases, MASP-2-related antibody-induced disease is a pulmonary disorder, including acute respiratory distress syndrome, transfusion-associated acute lung injury, acute lung ischemia / reperfusion injury, chronic obstructive pulmonary disease, asthma, Wegener's granulomatosis, antiglomerular basement membrane disease (Goodpasture's disease), meconium aspiration syndrome, aspiration pneumonia, bronchiolitis obliterans syndrome, idiopathic pulmonary fibrosis, burn-related acute lung injury, noncardiovascular pulmonary edema, transfusion-associated respiratory depression, and emphysema. In some cases, the MASP-2-related antibody-induced disease is an ex vivo inflammatory response induced by contact, and the method comprises treating a subject undergoing one of the following: hemodialysis, plasmapheresis, leukopheresis, extracorporeal membrane oxygenation (ECMO), heparin-induced LDL deposition e...

Claims

MP.1.0261. National Phase Reduced Claim Set (12 / 12 / 2018) 1 . A stable pharmaceutical formulation suitable for parenteral administration to a mammalian subject, comprising: (a) an aqueous solution comprising a buffer system having a pH of 5.0 to 7.0, wherein the buffer system comprises at least one buffering agent selected from the group consisting of citrate or histidine; (b) a monoclonal antibody or fragment thereof that specifically binds to human MASP-2 at a concentration of about 50 mg / mL to about 250 mg / mL, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and (ii) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3; and (c) a tonicity modifying agent in a sufficient amount for the formulation to be hypertonic; wherein the formulation has a viscosity of between 2 and 50 centipoise (cP), and wherein the formulation is stable when stored at between 2o C and 8o C for at least six months.2 . The pharmaceutical formulation of claim 1, wherein at least one or more of the following applies: (a) wherein the concentration of the antibody in the formulation is from about 100 mg / mL to about 225 mg / mL, or from about 150 mg / mL to about 200 mg / mL, or from about 175 mg / mL to about 195 mg / mL; (b) wherein the viscosity of the formulation is from about 2 cP to about 40 cP, or from about 2 cP to about 30 cP, or from about 2 cP to about 25 cP, or from about 2 cP to about 20 cP, or from about 2 cP to about 18 cP; (c) wherein the viscosity is less than about 25 cP, or such as less than about 20 cP, or such as less than about 18 cP; (d) wherein the concentration of the antibody is about 185 mg / mL; (e) wherein the formulation is stable when stored between 2°C and 8°C for at least 12 months; (f) wherein the injection glide force of the formulation is about 25 Newton or less when injected through a 27GA 1.25” needle at room temperature; and / or (g) wherein the injection glide force of the formulation is about 20 Newton or less when injected through a 25GA 1” needle at room temperature.3 . The pharmaceutical formulation of claim 1, wherein the at least one buffering agent is citrate, such as sodium citrate, such as wherein citrate is present in the solution at a concentration of 10 mM to 50 mM.4 . The pharmaceutical formulation of claim 1, wherein the tonicity modifying agent is an amino acid with a charged side chain selected from the group consisting of: (a) wherein the amino acid with a charged side chain is present in the formulation at a concentration of from about 150 mM to about 300 mM; (b) wherein the tonicity modifying agent is an amino acid with a negatively charged side chain; such as glutamate (c) wherein the tonicity modifying agent is an amino acid with a positively charged side chain, such as arginine or L-arginine-HCl, and (d) wherein arginine is present in the solution at a hypertonic level of from 200 mM to 300 mM.5 . The pharmaceutical formulation of claim 3, wherein the solution comprises about 20 mM citrate and has a pH from about 5.5 to about 6.5, optionally wherein the solution further comprises arginine at a concentration of about 200 mM.6 . The pharmaceutical formulation of claim 1, wherein the solution further comprises a surfactant at a concentration from about 0.001% (w / v) and about 0.1% (w / v), optionally wherein the surfactant is a nonionic surfactant such as a polysorbate or a poloxamer, e.g., polysorbate 807 . The pharmaceutical formulation of claim 1, wherein the formulation comprises: about 20 mM sodium citrate, about 200 mM L-arginine HCl, wherein the concentration of the antibody in the formulation is from about 175 mg / mL to about 195 mg / mL, and wherein the viscosity is less than about 25cP, optionally wherein the formulation further comprises from 0.001% w / v to 0.05% w / v polysorbate 80.8 . The pharmaceutical formulation of claim 1, wherein the formulation is sterile.9 . The pharmaceutical formulation of claim 1, wherein the monoclonal antibody is a full length monoclonal antibody, optionally wherein the antibody is a human IgG4 full length antibody, such as a human IgG4 antibody comprising a mutation in the hinge region.10 . The pharmaceutical formulation of claim 1, wherein one or more the following applies: (a) wherein the formulation does not include sucrose or sorbitol; (b) wherein the formulation does not include CaCl2 ; (c) wherein the formulation does not include MgCl2 ; (d) wherein the formulation does not include CaCl2 and wherein the formulation does not include MgCl2; and / or (e) wherein the formulation does not include a divalent cation additive.11 . The pharmaceutical formulation of claim 1, wherein the formulation is selected from the group consisting of: (i) a formulation comprising (a) polysorbate 80 at a concentration from about 0.01 to about 0.08% w / v; (b) L-arginine HCl at a concentration from about 150 mM to about 200 mM; (c) sodium citrate at a concentration from about 10 mM to about 50 mM; and (d) about 150 mg / mL to about 200 mg / mL of the antibody; and (ii) a formulation comprising (a) polysorbate 80 at a concentration of about 0.01 w / v; (b) L-arginine HCl at a concentration of about 200 mM; (c) sodium citrate at a concentration of about 20 mM; and (d) about 175 mg / mL to about 195 mg / mL of the antibody.12 . A stable aqueous pharmaceutical formulation suitable for parenteral administration to a mammalian subject, the formulation consisting essentially of: (a) polysorbate 80 at a concentration from about 0.01 to about 0.08% w / v; (b) L-arginine HCl at a concentration from about 150 mM to about 200 mM; (c) sodium citrate at a concentration from about 10 mM to about 50 mM; and (d) a monoclonal antibody or fragment thereof that specifically binds to human MASP-2 at a concentration of about 150 mg / mL to about 200 mg / mL, wherein said antibody or fragment thereof comprises (i) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and (ii) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3; wherein the formulation has a pH from about 5.0 to about 7.0, a viscosity of between 2 and 50 centipoise (cP), and wherein the formulation is stable when stored at between 2o C and 8o C for at least six months.13 . A sealed container containing a formulation according to Claim 1 or 12.14 . A subcutaneous administration device containing the formulation of Claim 1 or 12 therein.15 . A kit comprising a pre-filled container comprising the pharmaceutical formulation comprising the MASP-2 antibody of Claim 1 or 12 and instructions for use of the formulation, such as wherein the pre-filled container is selected from the group consisting of: a syringe, a pen injector, a sealed vial, an auto-injector and a pump device, optionally wherein the kit further comprises at least one injection device suitable for administering the formulation in the sealed vial to a human subject.16 . A pharmaceutical unit dosage form suitable for parental administration to a human, comprising a formulation according to claim 1 or 12 in a suitable container.17 . Use of a formulation of claim 1 or 12 in the manufacture of a medicament for treating a subject suffering from a MASP-2-dependent complement-associated disease or disorder.18 . The use of claim 17, wherein the formulation is suitable for subcutaneous administration.19 . The use of claim 18, wherein the formulation is contained within a pre-filled syringe.20 . A pharmaceutical composition for use in treating a patient suffering from, or at risk for developing a MASP-2-dependent complement-associated disease or disorder, wherein the composition is a sterile, single-use dosage form comprising from about 350mg to about 400mg of MASP-2 inhibitory antibody, wherein the composition comprises about 1.8mL to about 2.2 mL of a 185mg / mL antibody formulation, wherein the antibody comprises (i) a heavy chain variable region comprising the amino acid sequence set forth in SEQ ID NO:2 and (ii) a light chain variable region comprising the amino acid sequence set forth in SEQ ID NO:3, and wherein the composition is stable when stored at between 2°C and 8°C for at least six months.

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