Abstract: The present invention refers to a method for the separation of host cell proteins (HCPs), antibody fragments and low molecular weight substances from solutions containing antibodies.

Abstract: The present invention provides a sensitive and specific indirect homogeneous mobility shift assay using size exclusion chromatography to measure biologics such as vedolizumab and ustekinumab in a patient sample. The assays of the present invention are particularly advantageous for detecting the presence or level of biologics that target complex or large antigens including cell surface proteins, transmembrane proteins, heavily glycosylated proteins, and multimeric proteins, as well as antigens that cannot be purified, impure antigens, and partially or substantially purified antigens. The present invention also provides isolated soluble ?4?7 integrin heterodimers and isolated soluble IL-12p40 monomers that are suitable for use in the indirect assays described herein.

Abstract: Provided herein is a novel method of purifying an IgG antibody from a preparation by use of an electropositive membrane having a defined porosity.

Abstract: The present invention relates to a method for purifying an immunoglobulin, and more particularly, to a method for purifying an immunoglobulin, which comprises: dissolving immunoglobulin-containing plasma protein fraction I+II+III or fraction II+III; adding caprylate to the solution to cause precipitation; performing dialysis and concentration after removal of the precipitate; performing anion exchange resin and ceramic cation exchange resin purification processes to effectively remove a solvent and detergent added to inactivate viruses; and performing elution while maintaining salt concentration at a constant level to maintain the immunoglobulin polymer content at a low level.

Abstract: A method for conversion of an N-terminal glutamine and/or glutamic acid residue of a protein to pyro-glutamic acid within a purification process.

Abstract: Herein is reported a method for producing a polypeptide in monomeric form comprising the following step: recovering the polypeptide in monomeric form from an ion exchange chromatography material by applying a solution comprising a non-ionic polymer and an additive.

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: Methods of enhancing efficiency of downstream chromatography steps for purification of proteins comprising: (a) passing a composition comprising a polypeptide of interest and various contaminants through an ion exchange membrane, wherein the polypeptide and the membrane have opposite charge, at operating conditions comprised of a buffer having a pH sufficiently distinct from the pi of the polypeptide to enhance the charge of the polypeptide and a low ionic strength effective to prevent the shielding of charges by buffer ions, which cause the membrane to bind the polypeptide and at least one contaminant, (b) overloading the ion exchange membrane such that at least one contaminant remains bound to the membrane while the polypeptide of interest is primarily in the effluent; (c) collecting the effluent from the ion exchange membrane comprising the polypeptide of interest; (d) subjecting the membrane effluent comprising the polypeptide of interest to a purification step of similar charge as the previous membrane,

Abstract: The present invention relates to a method for the preparation of a solution of immunoglobulins based on an initial solution of immunoglobulins with a purity greater than or equal to 96% in the presence of a polyether or polymer of glycol, characterized in that it comprises the steps of: a) adding caprylic acid or salts of the same to the initial solution; b) adjusting the pH of the solution obtained in step a); c) incubating the solution obtained in step b) for the time and at a temperature necessary for the inactivation of enveloped viruses; d) performing a step of ultrafiltration/diafiltration on the solution obtained in step c).

Abstract: The present invention relates to a method for separating antibody isoforms using cation exchange chromatography and, more specifically, to a method for separating and purifying several isoforms, which are generated during an antibody production procedure, using a washing buffer for cation exchange chromatography.

Abstract: Disclosed here includes a method for purifying a biologic composition, comprising diafiltering the biologic composition into a composition comprising phosphate buffered saline (PBS) to obtain a purified composition. The method disclosed here can be particularly useful for removing one or more impurities from the biologic composition, such as bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane (Bis-tris).

Abstract: The present invention is directed to methods comprising the use of hydroxyapatite chromatography to separate a bispecific antibody from a solution that also comprises one or more byproducts specific to bispecific antibody production. Byproducts specific to the production of bispecific antibodies (bispecific antibody specific byproducts, “BASB”) include fragments of the bispecific antibody and heavier molecular weight variants of the antibody, wherein the fragment and/or variant comprises an Fc domain but does not exhibit affinity for the two different epitopes and/or antigens as exhibited by the desired bispecific antibody. Thus, the methods of the present invention comprise the separation of a bispecific antibody from one or more of its BASB. The hydroxyapatite chromatography methods of the invention may be used alone or may be further combined with standard purification processes and unit operations as is known in the art to achieve any level of purity of bispecific antibody necessary, e.g.

Abstract: The invention discloses a polypeptide with improved alkaline stability, which polypeptide comprises a mutant of a B or C domain of Staphylococcus Protein A (SpA), as specified by SEQ ID NO 1 or SEQ ID NO 2, or of Protein Z, as specified by SEQ ID NO 3, comprising at least the mutation wherein the glutamine residue at position 9 has been mutated to a tryptophan, leucine, glutamic acid, valine or lysine. The invention also discloses multimers of the polypeptide, as well as separation matrices comprising the multimers or polypeptides.

Abstract: Affinity ligands useful for mild elution affinity chromatography, including affinity ligands specific for immunoglobulins M, A, and E, are disclosed as are method of identifying and using such affinity ligands.

Abstract: The present invention provides novel and improved protein purification processes which incorporate certain types of carbonaceous materials and result in effective and selective removal of certain undesirable impurities without adversely effecting the yield of the desired protein product.

Abstract: The present invention relates to a method for purifying an immunoglobulin, and more particularly, to a method for purifying an immunoglobulin, which comprises: dialyzing and concentrating an immunoglobulin-containing plasma protein fraction II paste; removing thrombotic substances from the dialyzed and concentrated fraction by a purification process using ceramic cation exchange resin; and performing elution while maintaining salt concentration at a constant level to maintain the polymer content of the immunoglobulin at a low level. When the immunoglobulin purification method according to the present invention is used, the efficiency with which impurities and thrombotic substances are removed can be increased and the polymer content of the immunoglobulin can be maintained, and thus a stable immunoglobulin with improved quality can be produced.

Abstract: The present invention relates to a purification and concentration method for proteins and antibodies. Particularly the present invention relates to a continuous surfactant based phase separation method for recovering hydrophobin fusion proteins, and for recovering target molecules, such as antibodies, directly from a liquid by using phase separation and hydrophobin-Protein A fusion technologies.

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.