Abstract: The invention relates to a process for inactivating proteases by repeatedly changing the pH in the cell culture supernatant at the start of the process for the purification of biopharmaceuticals. The pH is adjusted first to 3-5, and then to 7-9.

Abstract: The present invention relates to methods of depleting impurities, in particular host cell proteins (HCP) and DNA from cell culture supernatants by means of protein A chromatography using a novel washing buffer.

Abstract: The present invention relates to methods of depleting impurities, in particular host cell proteins (HCP) and DNA from cell culture supernatants by means of protein A chromatography using a novel washing buffer.

Abstract: The invention relates to a process for inactivating proteases by repeatedly changing the pH in the cell culture supernatant at the start of the process for the purification of biopharmaceuticals. The pH is adjusted first to 3-5, and then to 7-9.

Abstract: The present application discloses a solid support material having covalently immobilized thereon an affinity ligand, said ligand comprising one or more hydrophobic functional group(s) and one or more cationic functional group(s) or one or more heteroaromatic functional group(s), wherein at least one hydrophobic functional group is separated from at least one cationic/heteroaromatic functional group by a through bond distance of from 5 ? to 20 ?, wherein said ligand has a molecular weight of from 120 Da to 5,000 Da. Typically, the affinity resin has a binding capacity larger than 5 mg monoclonal antibody per mL of affinity resin. A method for the isolation of biomolecules, such as proteins, in particular antibodies, such as monoclonal antibodies, or derivatives thereof, is also disclosed.