1617results about "Serum immunoglobulins" patented technology

A bispecific antibody format providing ease of isolation is provided, comprising immunoglobulin heavy chain variable domains that are differentially modified in the CH3 domain, wherein the differential modifications are non-immunogenic or substantially non-immunogenic with respect to the CH3 modifications, and at least one of the modifications results in a differential affinity for the bispecific antibody for an affinity reagent such as Protein A, and the bispecific antibody is isolable from a disrupted cell, from medium, or from a mixture of antibodies based on its affinity for Protein A.

Methods for obtaining a protein by culture of hybridoma cells, wherein said protein is an immunoglobulin, are disclosed. The methods involve culturing animal hybridoma cells in continuous presence of an alkanoic acid or salt thereof, which enhances protein production, wherein said alkanoic acid or salt thereof is present at 2 concentration range of 0.1 mM to 200 mM.

A separation medium having a base matrix and matrix-bound groups which exhibit recombinant Protein A containing a cysteine. The groups are of formula:where B is a bridge which binds to the base matrix and X includes a heteroatom N or S from rProtein A-cys. In a preferred embodiment X is a thioether sulphur and / or a secondary amine (-NH-). An alternative embodiment features a variant of Protein A in which the C-terminal residue is cysteine.

A method for purifying a polypeptide by ion exchange chromatography is described which involves changing the conductivity and / or pH of buffers in order to resolve a polypeptide of interest from one or more contaminants.

The present invention relates to a process for purifying an antibody having a desired property, which comprises using a substance having an affinity to a carbohydrate binding to the antibody; a medicament comprising, as an active ingredient, the antibody purified by the process; and a method for diagnosing or preventing various diseases, which comprises using a substance having an affinity to a carbohydrate binding to an antibody.

The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.

Problems to be Solved: The present invention provides a simpler and less expensive method for purifying physiologically active proteins, especially antibodies, which can ensure removal of impurities such as DNA contaminants and viruses, and which can minimize a loss of physiologically active proteins. Means for Solving the Problems: A method for removing impurities in a physiologically active protein-containing sample, which comprises the following steps: 1) allowing the physiologically active protein-containing sample to be converted into an aqueous solution of low conductivity at a pH below the isoelectric point of the physiologically active protein; and 2) removing the resulting particles.

The invention concerns a method for preparing human immunoglobulin concentrates for therapeutic use, from plasma or a plasma fraction. The method comprises pre-purification and a single anion-exchange chromatography carried out at alkaline pH, thereby enabling the immunoglobulins to be retained on the chromatographic support and fractionated. The method enables to obtain IgG, IgA and IgM concentrates.

A method for reducing leaching of protein A during protein A affinity chromatography is described which involves reducing temperature or pH of, or by adding one or more protease inhibitors to, a composition that is subjected to protein A affinity chromatography.

The present invention provides stabilized preparations containing an antibody in a glycine buffer and / or a histidine buffer and also provides processes for preparing a protein-containing stabilized preparation, comprising adjusting the pH with a basic amino acid or a basic amino acid derivative or a salt thereof.

Methods for the high yield production of antibody Fv-containing polypeptides, especially Fab′ and F(ab′)2 antibody fragments are provided. Expression of heavy and light chain Fv in a microbial secretory system is followed by recovery of Fv from the periplasm under conditions that maintain a cysteine residue as a free thiol. The free thiol is reacted with free thiol of an antibody fragment of the same or differing specificity, or with agents such as diagnostic labels or therapeutic moieties. The products offer advantages of homogeneity and purity not available through the use of known methods for preparing such derivatives.

A method for reducing leaching of protein A during protein A affinity chromatography is described which involves reducing temperature or pH of, or by adding one or more protease inhibitors to, a composition that is subjected to protein A affinity chromatography.

A novel method for selectively removing leaked protein A from antibody purified by means of protein A affinity chromatography is disclosed.

A method is disclosed for separating a polypeptide monomer from a mixture comprising dimers and / or multimers. The method comprises applying the mixture to either a cation-exchange chromatography resin or an anion-exchange chromatography resin and eluting the mixture at a gradient of about 0-1 M of an elution salt, wherein the monomer is separated from the dimers and / or multimers present in the mixture.

The present invention relates to a new and improved method for preparing a highly concentrated immunoglobulin composition from pooled plasma for subcutaneous injection. A composition comprising 20% or more immunoglobulin suitable for subcutaneous use is also described.

A method for purifying a polypeptide by ion exchange chromatography is described which involves changing the conductivity and / or pH of buffers in order to resolve a polypeptide of interest from one or more contaminants.

The invention discloses methods for the generation of chimaeric human-non-human antibodies and chimaeric antibody chains, antibodies and antibody chains so produced, and derivatives thereof including fully humanised antibodies; compositions comprising said antibodies, antibody chains and derivatives, as well as cells, non-human mammals and vectors, suitable for use in said methods.

The invention herein provides a method for recovering a polypeptide comprising exposing a composition comprising a polypeptide to a reagent which binds to, or modifies, the polypeptide, wherein the reagent is immobilized on a solid phase; and then passing the composition through a filter bearing a charge which is opposite to the charge of the reagent in the composition, so as to remove leached reagent from the composition.

A novel method for selectively removing leaked protein A from antibody purified by means of protein A affnitiy chromatography is disclosed.

The present invention provides liquid formulations of antibodies or antibody fragments that immunospecifically bind to an IL-9 polypeptide, which formulations exhibit stability, low to undetectable levels of aggregation, and very little to no loss of the biological activities of the antibodies or antibody fragments, even during long periods of storage. In particular, the present invention provides liquid formulations of antibodies or fragments thereof that immunospecifically bind to an IL-9 polypeptide, which formulations are substantially free of surfactants, sugars, sugar alcohols, amino acids other than histidine (preferably with pKa values of less than 5 and above 7), and / or other common excipients. Furthermore, the invention provides methods of preventing, treating or ameliorating a disease or disorder associated with or characterized by aberrant expression and / or activity of an IL-9 polypeptide, a disease or disorder associated with or characterized by aberrant expression and / or activity of the IL-9R or one or more subunits thereof, an autoimmune disease, an inflammatory disease, a proliferative disease, or an infection (preferably, a respiratory infection), or one or more symptoms thereof, utilizing the liquid formulations of the present invention.

The present invention describes the use of porous metal oxides for the preparative purification of antibodies and biomolecules within a range of particle physical characteristics. Typically, particles from 15 to 100 microns in average diameter with pores sizes ranging from 400 to 600 angstroms and surface areas from 10 to 50 square meters per gram, and pore volumes from 0.1 to 0.4 mL / gram can be used for purification processes. The metal oxide particles that fall within this range of physical properties show enhanced utility and greater chromatographic capacity for antibodies than materials oxide particles falling outside of this range. Metal oxides such as zirconia, titania and alumina can all be modified with a multi-Lewis base moiety such as an organophosphate ethylenediamine-N,N-tetra(methylenephosphonic) acid (EDTPA), to produce a bio-compatible purification media for, biomolecules.

The present invention provides a pharmaceutical formulation comprising an antibody or antigen-binding fragment thereof that exhibits high stability; along with methods of use thereof.

An improved process for the purification of antibodies from human plasma or other sources is disclosed. The process involves suspension of the antibodies at pH 3.8 to 4.5 followed by addition of caprylic acid and a pH shift to pH 5.0 to 5.2. A precipitate of contaminating proteins, lipids and caprylate forms and is removed, while the majority of the antibodies remain in solution. Sodium caprylate is again added to a final concentration of not less than about 15 mM. This solution is incubated for 1 hour at 25° C. to effect viral inactivation. A precipitate (mainly caprylate) is removed and the clear solution is diluted with purified water to reduce ionic strength. Anion exchange chromatography using two different resins is utilized to obtain an exceptionally pure IgG with subclass distribution similar to the starting distribution. The method maximizes yield and produces a gamma globulin with greater than 99% purity. The resin columns used to obtain a high yield of IgG retain IgM and IgA. IgA and IgM may be eluted from these resins in high yield and purity.

A method for purifying proteins by Protein A chromatography is described which comprises removing contaminants by washing the solid phase with various intermediate wash buffers.

The invention belongs to the biotechnology field, and in particular relates to escherichia coli TolC antigen and antibody. The antibody has the specificity aiming to a sequence shown by SEQ ID NO:1. The invention also provides a gene sequence for encoding the escherichia coli TolC antigen and application of the antibody to preparing a drug for inhibiting the bacterial resistance. The anti-TolC fragment SNGYRDANGI antibody enhances the sensitivity of bacteria to antibiotic and can specifically and efficiently inhibit the functions of drug resistance outer membrane protein of escherichia coli, thereby solving the problem of the bacterial resistance. Compared with the traditional antibody, the antibody has higher safety and operability on the application of the bacterial resistance drug.

The object of the present invention is the oral administration of animal immunoglobulins for the treatment of gastrointestinal disorders caused by bacterial and / or yeast overgrowth. Immunoglobulins derived from the blood, plasma or serum of animals, such as cow, goats, sheep and pigs, contain a broad spectrum of antibodies to bacteria and yeast that afflict the gastrointestinal tract of human patients.