The present invention relates to: a method of purifying an antibody, which can prepare a desired antibody with high purity and high quality by removing impurities without using an expensive protein A column, and particularly, can purify an antibody in a high yield while greatly reducing an amount (volume) of a buffer used in an elution process; and an antibody prepared by the method.

Provided herein are methods of performing viral filtration on a fluid including a recombinant antibody, and the use of these methods in methods of manufacturing or producing the recombinant antibody.

A hybridoma cell line of secreting cyproheptadine monoclonal antibodies with a preservation number of CGMCC No. 14699 belongs to the field of food safety immunological detection. BALB/c mice are immunized through one time immunization with complete freund's adjuvant, three times of booster immunization with incomplete freund's adjuvant and one time of rush immunization with cyproheptadine complete antigen without adjuvant; the spleen cells from BALB/C mice immunized with high potency and low value of IC50 are fused with murine myeloma cells; and then the hybridoma cell line is obtained through indirect competitive ELISA screening and three sub-clones. The monoclonal antibody secreted by this cell line has good specificity and detection sensitivity to cyproheptadine (value of IC50 is 0.37 ng/ml), being suitable for detection of cyproheptadine in food.

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.

A composition comprising a main species HER2 antibody that binds to domain II of HER2 and acidic variants thereof is described. Pharmaceutical formulations comprising the composition, and therapeutic uses for the composition are also disclosed.

The disclosure relates to methods to control trace metals during production of anti-CD38 antibodies, drug substances and drug products generated using the methods, and uses of the generated drug substances and drug products.

The present disclosure relates to, inter alia, a method of quantitating an amount of an antibody molecule from a mixture comprising two or more antibody molecules, comprising separating each of the two or more antibody molecules from the mixture by hydrophobic interaction chromatography high performance liquid chromatography (HIC-HPLC) and quantitating an amount of each antibody molecule, wherein the molecular weight of each antibody molecule is within 15 kDa of any other antibody molecule in the mixture and either each antibody molecule is different from another antibody molecule in the mixture by more than about 0.25 unit on the Kyte & Doolittle hydropathy scale or each of the antibody molecules when run alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

The present invention relates to a method of preparing a population of antibodies, whereby a desired high-purity and high-quality population of antibodies can be prepared by removing impurities without using an expensive protein A column, and in particular, production costs can be significantly reduced while achieving process automation; and a population of antibodies prepared thereby.

A protein purification process with virus inactivation or removal uses caprylic acid (octanoic acid) at acidic pH. The method comprises caprylic acid treatment as part of the chromatographic step so as to perform viral inactivation without a discontinuous process and without the requirement of attention by personnel, particularly when the pH adjustment of the eluate is performed automatically by eluting into buffer. The method of the invention further results in mycoplasmas being inactivated, and reduced impurities like Host Cell Protein (HCP).

Aspects of the present disclosure relate to a method of regenerating a hydrophobic interaction chromatography column to which a load mass has been applied, the method comprising passing one or more column volumes of an alkaline solution through hydrophobic interaction media within the column, wherein the alkaline solution exhibits a pH of between about 10 and about 14, and a conductivity of between 0.5 mS/cm and about 10 mS/cm, wherein material bound to the hydrophobic interaction media is removed. In some cases, the alkaline solution may include sodium hydroxide at a concentration of between, e.g., about 0.1 mM and 10 mM.