Abstract: Herein is reported a method for the purification of an antibody directly captured from clarified cell culture supernatants using Streamline CST and/or Capto MMC, wherein especially product related (aggregates and fragments) and process related impurities (host cell protein, media components) could efficiently be removed, resulting in a preparation with a purity comparable to classical protein A affinity chromatography.

Abstract: Herein is reported a method for the purification of a protein comprising erythropoietin and a single poly (ethylene glycol) residue from reaction by-products or not reacted starting material by a cation exchange chromatography method. It has been found that by employing a cation exchange Toyopearl® SP-650 chromatography material and employing a second wash step with an increased pH value compared to the first wash step a fusion protein of erythropoietin and a single poly (ethylene glycol) residue can be obtained in a single step with high purity and yield and suitability for large scale applications.

Abstract: Herein is reported a method for the enzymatic preparation/production of an antibody with a modified glycosylation in the Fc-region comprises the steps of incubating an antibody that has a glycosylation in the Fc-region with one or more enzymes for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating in one or more chromatography steps the antibody with a modified glycosylation in the Fc-region from the one or more enzymes and thereby producing the antibody with a modified glycosylation in the Fc-region and one or more recycled enzymes, and repeating the incubating step with the one or more recycled enzymes at least once.

Abstract: Herein is reported a method for producing or purifying an antibody using a mixed mode chromatography material that comprises ion exchange functional groups and hydrophobic interaction functional groups (MM HIC/TEX) operated in flowthrough mode, wherein the antibody is a hydrophilic antibody, and the antibody is applied in a solution comprising the antibody and an antichaotropic salt to the MM HIC/IEX chromatography material.

Abstract: Herein is reported a method for the final filtration of concentrated polypeptide solutions comprising the combination of two immediately consecutive filtration steps with a first filter of 3.0 ?m and 0.8 ?m pore size and a second filter of 0.45 ?m and 0.22 ?m pore size.

Abstract: Herein is reported a method for the purification of a protein comprising erythropoietin and a single poly (ethylene glycol) residue from reaction by-products or not reacted starting material by a cation exchange chromatography method. It has been found that by employing a cation exchange Toyopearl® SP-650 chromatography material and employing a second wash step with an increased pH value compared to the first wash step a fusion protein of erythropoietin and a single poly (ethylene glycol) residue can be obtained in a single step with high purity and yield and suitability for large scale applications.

Abstract: Herein is reported a method for the final filtration of concentrated polypeptide solutions comprising the combination of two immediately consecutive filtration steps with a first filter of 3.0 ?m and 0.8 ?m pore size and a second filter of 0.45 ?m and 0.22 ?m pore size.

Abstract: Herein is reported the use of an immobilized non-covalent complex of a neonatal Fc receptor (FcRn) and beta-2-microglobulin (b2m) as affinity chromotography ligand in general and, for example, for the determination of the in vivo half-live of an antibody by determining the ratio of the retention times of the antibody and a reference antibody.

Abstract: Herein is reported a method for producing an antibody comprising the steps of forming an antibody-antibody light chain affinity ligand complex, wherein the antibody light chain affinity ligand is immobilized on a solid phase, by applying a solution comprising the antibody to the immobilized antibody light chain affinity ligand, and incubating the complex formed in the previous step with one or more enzymes to modify the glycosylation of the antibody, thereby producing the antibody.

Abstract: Herein is reported a method for the final filtration of concentrated polypeptide solutions comprising the combination of two immediately consecutive filtration steps with a first filter of 3.0 ?m and 0.8 ?m pore size and a second filter of 0.45 ?m and 0.22 ?m pore size.

Abstract: The present invention generally relates to the provision of means and methods for preparing protein compositions. The invention provides a method comprising the steps of (i) contacting a starting composition comprising a protein with a hydrolase inhibitor, wherein the hydrolase inhibitor is immobilized on a solid carrier; (ii) recovering a composition comprising the protein. Furthermore, the invention relates to a method for preparing a protein formulation comprising the steps of (i) contacting a starting composition comprising a protein with a hydrolase inhibitor, wherein the hydrolase inhibitor is immobilized on a solid carrier; (ii) recovering a composition comprising the protein, wherein the method for preparing the protein formulation further comprises adding a surfactant, preferably a fatty acid ester, to the composition comprising the protein.

Abstract: Herein is reported a method for the purification or production of a therapeutic polypeptide using the same depth filter multiple times, i.e. a depth filter which has been used before and has been regenerated. Reported herein is a method for purifying or producing a therapeutic polypeptide, characterized in that the method comprises the following steps: a) filtering an aqueous composition containing said therapeutic polypeptide and impurities through a depth filter, recovering the flow-through and thereby obtaining said purified therapeutic polypeptide, b) contacting said depth filter with a regeneration solution and thereby regenerating the depth filter, and c) repeating steps a) and b) one or more times.

Abstract: Herein is reported the use of an immobilized non-covalent complex of a neonatal Fc receptor (FcRn) and beta-2-microglobulin (b2m) as affinity chromatography ligand in general and, for example, for the determination of the in vivo half-live of an antibody by determining the ratio of the retention times of the antibody and a reference antibody.

Abstract: Herein is reported a method for determining the presence of hydrolase activity in a sample by incubating the sample in a buffered solution, which comprises an artificial hydrolase substrate that comprises an ester bond covalently linking an alcohol residue, which is conjugated to a label for removal, and a carboxylic acid residue, which is conjugated to a capture and detection label, as well as bovine serum albumin, and thereafter determining or quantifying, respectively, the released carboxylic acid in the free alcohol depleted incubation mixture.

Abstract: Herein is reported a method for the enzymatic production of an antibody with a modified glycosylation in the Fc-region comprising the steps of incubating the antibody light chain affinity ligand-bound monoclonal antibody with a glycosylation in the Fc-region with a first enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region, recovering the antibody from the antibody light chain affinity ligand, incubating the recovered antibody in solution with a second enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating the antibody with the modified glycosylation in the Fc-region from the second enzyme in a cation exchange chromatography, and thereby producing the antibody with a modified glycosylation in the Fc-region.

Abstract: The present disclosure provides purification platforms comprising a depth filter step and/or a hydrophobic interaction chromatography (HIC) step. Also disclosed herein are methods of using the purification platforms described herein and compositions obtained therefrom, such as pharmaceutical compositions.

Abstract: The current invention reports a method for purifying an antibody by reducing the content of a host cell protein. The method employs a wash step with a low conductivity aqueous solution in an affinity chromatography.

Abstract: Herein is reported a method for purifying a polypeptide comprising the steps of i) applying a solution comprising the polypeptide to an ion exchange chromatography material, and ii) recovering the polypeptide with a solution comprising a denaturant and thereby purifying the polypeptide, whereby the ion exchange chromatography material comprises a matrix of cross-linked poly (styrene-divinylbenzene) to which ionic ligands have been attached, and wherein the solution comprising the polypeptide applied to the ion exchange chromatography material is free of the denaturant and the polypeptide adsorbed to the ion exchange chromatography material is recovered with a solution comprising a denaturant at a constant conductivity.

Abstract: Herein is reported a method for producing a bispecific antibody comprising a first antigen-binding site that specifically binds to a first antigen and a second antigen-binding site that specifically binds to a second antigen comprising the following steps a) cultivating a cell comprising a nucleic acid encoding the bispecific antibody, b) recovering the bispecific antibody from the cell or the cultivation medium, c) contacting the bispecific antibody with an affinity chromatography material, d) washing the affinity chromatography material with a low conductivity aqueous solution, wherein the low conductivity aqueous solution has a conductivity value of about 0.5 mS/cm or less, e) recovering the bispecific antibody from the affinity chromatography material, f) performing a further chromatography step and thereby producing the bispecific antibody.

Abstract: Herein is reported a method for producing a human IgG4 or IgG1 isotype antibody comprising the following steps a) cultivating a cell comprising a nucleic acid encoding a human IgG4 or IgG1 isotype antibody, b) recovering the human IgG4 or IgG1 isotype antibody from the cell or the cultivation medium, c) contacting the human IgG4 or IgG1 isotype antibody with a protein A chromatography material, d) washing the protein A chromatography material with an aqueous solution comprising Histidine and Tris, e) recovering the human IgG4 or IgG1 isotype antibody from the protein A chromatography material and thereby producing the human IgG4 or IgG1 isotype antibody.