Abstract: The current invention reports a method for purifying an immunoglobulin, wherein the method comprises applying an aqueous, buffered solution comprising an immunoglobulin in monomeric and in aggregated form to a cation exchange material under conditions whereby the immunoglobulin in monomeric form does not bind to the cation exchange material, and recovering the immunoglobulin in monomeric form from the solution after the contact with the cation exchange 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: The present invention describes a tire, which shows the insertion of a passive UHF RFID tag at its moment of manufacture, in which said tag is affixed on top of the metallic part of the referred tire, more specifically on the bead rim, with the purpose of reducing the mechanical stress of the tire in question and allowing its tracking in the manufacturing chain since its first manufacturing stages.

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: 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 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 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: The current invention reports a method for purifying an immunoglobulin, wherein the method comprises applying an aqueous, buffered solution comprising an immunoglobulin in monomeric and in aggregated form to a cation exchange material under conditions whereby the immunoglobulin in monomeric form does not bind to the cation exchange material, and recovering the immunoglobulin in monomeric form from the solution after the contact with the cation exchange material.

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 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 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 SP Sephacryl™ S 500 HR chromatography material conditioned to a conductivity of 21 mS/cm and a linear gradient elution a fusion protein of erythropoietin and a single poly (ethylene glycol) residue can be obtained in a single step with high purity and yield.

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: The current invention is directed to a chromatography column separator which separates the chromatography column in an upper chromatography column chamber and a lower chromatography column chamber, and which has a variable position within the chromatography column, and which is embedded by the chromatography material. The separator allows the replacement of the chromatography material in the upper chromatography column chamber without the need to replace the chromatography column material in the lower chromatography column chamber and it allows also the combination of two different chromatography materials with different chromatographical functional groups in one chromatography column.

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.

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: 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 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: A method for the purification of immunoglobulins by ion exchange chromatography is described. The chromatographic method uses a weak ion exchange resin and a single step elution process for the purification of an immunoglobulin. Additionally a method for the determination of the salt concentration for the single step elution of an immunoglobulin from an ion exchange resin is described.

Abstract: The current invention reports a method for purifying an immunoglobulin, wherein the method comprises applying an aqueous, buffered solution comprising an immunoglobulin in monomeric and in aggregated form to a cation exchange material under conditions whereby the immunoglobulin in monomeric form does not bind to the cation exchange material, and recovering the immunoglobulin in monomeric form from the solution after the contact with the cation exchange material.