Abstract: Described herein is a method for separating a recombinantly produced polypeptide from host cell protein. The method includes a step of loading a clarified cell culture supernatant that includes the recombinantly produced polypeptide and the HCP onto a Protein A chromatography column and washing the Protein A chromatography column with a wash buffer comprising a fatty acid having a chain length of at least about 6 carbon atoms, or a fatty acid salt thereof to remove HCP and then recovering the recombinantly produced polypeptide.

Abstract: A method is provided for purifying a recombinant protein from a mixture comprising the recombinant protein and related proteins, comprising the steps of: A. using a first equilibrating buffer in a first conductivity and pH to make the recombinant protein bind to an ion exchange medium; B. using a second equilibration buffer in a second conductivity and pH to continually equilibrate the ion exchange medium bound to the protein; C. using a washing liquid in a third conductivity and a gradually increasing pH to wash the ion-exchange medium, and eluting the first category-related proteins; D. using a first eluent in a fourth conductivity and pH to elute the ion exchange medium, and eluting the target recombinant protein; and E. using a second eluent in a fifth conductivity and pH to continually elute the ion exchange medium, and eluting the second category-related proteins.

Abstract: The present invention relates to a selectively soluble polymer capable of binding to a desired molecules in an unclarified mixture containing various biological materials and the methods of using such a polymer to purify a molecule from such a mixture. The polymer is soluble in the mixture under a certain set of process conditions such as pH or temperature and/or salt concentration and is rendered insoluble and precipitates out of solution upon a change in the process conditions. The polymer is capable of binding to the desired molecule (protein, polypeptide, etc) and remains capable of binding to that molecule even after the polymer is precipitated out of solution. The precipitate can then be filtered out from the remainder of the stream and the desired biomolecule is recovered such as by elution and further processed.

Abstract: A new platform method to purify plant-based monoclonal antibodies is provided. Such a method includes an antibody purification platform that involves a standardized procedure for the production of a wide array of different antibodies within a simplified context. The versatility of the overall purification process accords a one-size-fits-all approach for myriad antibody products and includes plant tissue harvesting, extraction and clarification, filtrate generation, a succession of column chromatography procedures, and buffer exposure to provide the desired monoclonal antibodies in proper filtered and purified form for further incorporation and/or use within medicaments and other formulations. Thus, the purified monoclonal antibodies produced thereby such a method are also encompassed within this invention.

Abstract: A multimeric immunoglobulin-binding protein having improved properties as an affinity ligand for affinity chromatography, and an insoluble support immobilizing such a multimer. The immunoglobulin-binding protein is represented by the formula: (R1)n-(R2)m, or (R2)m-(R1)n. R2 is an immunoglobulin-binding domain including an amino acid residue that covalently bonds to an insoluble support upon immobilization reaction with the insoluble support, and R1 is an immunoglobulin-binding domain without containing an amino acid residue the presence of which in the sequence compared to when it is absent in the sequence reduces the immunoglobulin-binding activity of the support yielded by the immobilization reaction. The immunoglobulin-binding protein satisfies: (1) n is an integer of 5 to 9; (2) m is an integer of 1 or 2; (3) the n (R1) domains may or may not have the same sequence; and (4) the total number of domains (n+m) is 6 to 10.

Abstract: The invention discloses an immunoglobulin-binding protein comprising one or more mutated immunoglobulin-binding domains (monomers) of staphylococcal Protein A (E, D, A, B, C) or protein Z or a functional variant thereof, wherein in at least one of the one or more mutated monomers, the asparagine or histidine at the position corresponding to H18 of the B domain of Protein A or of Protein Z has been deleted or substituted with a first amino acid residue which is not proline or asparagine and wherein, if the amino acid residue at position 57 is proline and the amino acid residue at position 28 is asparagine, then the amino acid residue at the position corresponding to H18 of the B domain of protein A or of protein Z is not serine, threonine or lysine.

Abstract: The present invention relates to a process for the purification of an antibody fragment from a periplasmic cell extract comprising a first cation exchange chromatography step and a second anion exchange chromatography step.

Abstract: A method of purifying a target protein includes contacting a cell culture harvest or a protein preparation including at least one target protein with at least one fatty acid having 8 to 10 carbon atoms to form a mixture, contacting the mixture with one or more solids to form a mixture, the one or more solids comprise a cationic functional group, a metal binding functional group, or both, the metal binding functional group including a nitrogen-containing moiety selected from (1) a polyamine, (2) an imine, (3) an N-heterocycle, (4) an amino acid, (5) an N-hydroxyamide, (6), an arylamine, and combinations thereof, and separating solid materials after contacting the mixture with the one or more solids to provide a solution comprising the target protein.

Abstract: A method of purifying a target antibody includes contacting a cell culture harvest or a protein preparation including at least one target antibody with at least one fatty acid having 7 to 10 carbon atoms to form a mixture, contacting this mixture with allantoin, and then separating solid materials to provide a solution comprising the target antibody. Solid materials can be removed by filtration, sedimentation or centrifugation, and the fatty acids can be enanthic, caprylic, pelargonic, nonenoic or capric acid. The invention is also directed to kits used to facilitate this method of antibody purification.

Abstract: The invention relates to a modified process for the purification of IgG, improving the yield of IgG per liter of starting material without compromising the quality of the product.

Abstract: 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.

Abstract: Processes and methods of purifying or separating Single Domain Antigen Binding (SDAB) molecules that include one or more single binding domains (e.g., one or more nanobody molecules), substantially devoid of a complementary antibody domain and an immunoglobulin constant region, using Protein A-based affinity chromatography, are disclosed.

Abstract: Herein is reported a method for producing an antibody preparation comprising the steps of a) applying a buffered solution comprising different isoforms of an antibody to a cation exchange chromatography material, b) applying a first solution with a first conductivity to the cation exchange chromatography material, whereby the antibody isoforms remain bound to the cation exchange chromatography material, and c) applying a second solution with a second conductivity to the cation exchange chromatography material and thereby obtaining the antibody preparation, whereby the conductivity of the second solution exceeds the conductivity of the first solution by not more than 10%.

Abstract: Provided herein are methods for refolding denatured protein (e.g., from inclusion bodies) that do not require the use of a denaturing agent. Exemplary methods use a high pH for solubilizing denatured protein, followed by a decrease in pH for refolding the proteins.

Abstract: The present invention relates to a method of purifying an antibody with high purity and high quality by removing impurities by sequential use of a cation-exchange column, a culture supernatant multilayer filter and an anion-exchange column without using a protein-A column that is an affinity chromatography column which is generally used for antibody purification.

Abstract: The invention provides methods of purifying antibodies using various antibody-specific purification media to rapidly and efficiently separate mixtures of antibodies, antibody fragments and/or antibody components to isolate a desired antibody product from the mixture. The invention relates to the purification of bispecific monoclonal antibodies carrying a different specificity for each binding site of the immunoglobulin molecule, e.g., antibodies composed of a single heavy chain and two different light chains, one containing a Kappa constant domain and the other a Lambda constant domain, including antibodies of different specificities that share a common heavy chain. The invention also provides the methods of efficiently purifying intact antibodies by separating the intact antibody from non-intact antibodies including free light chains.

Abstract: Methods for the improved purification of antibodies and other proteins from protein preparations including the steps of conditioning the protein preparation by contacting it with multivalent organic ions, then applying the conditioned preparation to an adsorptive chromatography medium.

Abstract: Various aspects and embodiments of the present disclosure relate to the purification antibodies by hydrophobic interaction chromatography under no-salt conditions.

Abstract: The present invention relates to a method for the separation of antibodies, specifically antibodies having different degrees of fucosylation. The method is based on binding affinity of antibodies to Fc receptors. The invention further relates to the use of Fc receptors for the separation of antibodies having different degrees of fucosylation.

Abstract: A method for the purification of a desired protein from a protein preparation includes conditioning the protein preparation by treatment with soluble organic multivalent ions, immobilized organic multivalent ions, or both, optionally in the presence of supersaturated allantoin, thereby removing at least 90% of chromatin, then (1) precipitating the desired protein with a nonionic organic polymer in the presence of non-protein-precipitating salts at greater than physiological concentration to provide a precipitate of the desired protein; or (2) precipitating the desired protein with a nonionic organic polymer in the absence of non-precipitating salts at greater than physiological concentration to provide a precipitate and subsequently washing the precipitate with a nonionic organic polymer in the presence of non-protein-precipitating salts at greater than physiological concentration.