Abstract: A method for purifying a protein comprising an antibody, antibody fragment, or immunoglobulin single variable domain, from a solution containing at least one contaminant by superantigen chromatography comprising: a) adsorbing the protein to the superantigen immobilized on a solid support; b) removing the at least one contaminant by contacting the immobilized superantigen containing the adsorbed protein with a first wash buffer comprising an aliphatic carboxylate; and c) eluting the protein from the superantigen immobilized on the solid support.

Abstract: A method for purifying a protein comprising an antibody, antibody fragment, or immunoglobulin single variable domain, from a solution containing at least one contaminant by superantigen chromatography comprising: a) adsorbing the protein to the superantigen immobilized on a solid support; b) removing the at least one contaminant by contacting the immobilized superantigen containing the adsorbed protein with a first wash buffer comprising an aliphatic carboxylate; and c) eluting the protein from the superantigen immobilized on the solid support.

Abstract: The present invention relates to a method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising: (a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising caprylate and arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

Abstract: The present invention relates to a method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising: (a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising caprylate and arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

Abstract: A method of purifying a recombinant polypeptide from a Host Cell Protein (HCP), wherein the amino acid sequence of the recombinant polypeptide comprises a cathepsin L cleavage site is provided. The method includes: (a) applying a solution containing the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer containing caprylate and arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support. A method of purifying an anti-OX40 antigen binding polypeptide from a Host Cell Protein (HCP) is also provided.

Abstract: A method for purifying a protein comprising an antibody, antibody fragment, or immunoglobulin single variable domain, from a solution containing at least one contaminant by superantigen chromatography comprising: a) adsorbing the protein to the superantigen immobilized on a solid support; b) removing the at least one contaminant by contacting the immobilized superantigen containing the adsorbed protein with a first wash buffer comprising an aliphatic carboxylate; and c) eluting the protein from the superantigen immobilized on the solid support.

Abstract: A method for purifying a protein comprising an antibody, antibody fragment, or immunoglobulin single variable domain, from a solution containing at least one contaminant by superantigen chromatography comprising: a) adsorbing the protein to the superantigen immobilized on a solid support; b) removing the at least one contaminant by contacting the immobilized superantigen containing the adsorbed protein with a first wash buffer comprising an aliphatic carboxylate; and c) eluting the protein from the superantigen immobilized on the solid support.

Abstract: A method for purifying a protein using a simplified, sodium chloride-free buffer system that consists of two components (acid and base pairs) for appropriate solution pH control; and a third component for ionic strength control, where the third component is the sodium salt conjugate base.

Abstract: A method for purifying a protein using a simplified, sodium chloride-free buffer system that consists of two components (acid and base pairs) for appropriate solution pH control; and a third component for ionic strength control, where the third component is the sodium salt conjugate base.

Abstract: The invention is directed to a method for producing a polypeptide composition comprising: combining a polypeptide with a volatile additive to form a liquid mixture and lyophilizing the liquid mixture to obtain a lyophilized polypeptide composition.

Abstract: A method for purifying a protein comprising an antibody, antibody fragment, or immunoglobulin single variable domain, from a solution containing at least one contaminant by superantigen chromatography comprising: a) adsorbing the protein to the superantigen immobilized on a solid support; b) removing the at least one contaminant by contacting the immobilized superantigen containing the adsorbed protein with a first wash buffer comprising an aliphatic carboxylate; and c) eluting the protein from the superantigen immobilized on the solid support.

Abstract: The invention is directed to a method for producing a polypeptide composition comprising: combining a polypeptide with a volatile additive to form a liquid mixture and lyophilizing the liquid mixture to obtain a lyophilized polypeptide composition.

Abstract: This invention relates to the use of amine, amino acid and amino acid ester mobile modifiers in normal phase chromatography to improve the resolution and or productivity of peptide and lipopeptide purification. This chromatographic method can be sued for either analytical or preparative scale purification.

Abstract: There is disclosed a process for purifying a natural product using a two-phase, multi-solvent system followed by vacuum concentration and back extraction. The method allows for the removal of impurities by controlling the polarity balance of a two-phase system by manipulating the proportions of the four solvents and subsequently the relative distribution of the product versus the impurities.

Abstract: There is disclosed a process for purifying a natural product using a two-phase, multi-solvent system followed by vacuum concentration and back extraction. The method allows for the removal of impurities by controlling the polarity balance of a two-phase system by manipulating the proportions of the four solvents and subsequently the relative distribution of the product versus the impurities.