A chromatography carrier capable of removing an antibody dimer from a solution containing an antibody monomer. The chromatography carrier includes a base carrier containing porous particles and a hydrophobic ligand bound to the base carrier, and has an electric conductivity of 34 mS/cm or less measured by a gradient elution test. The porous particles preferably have an average particle diameter of 66 to 150 μm, and the hydrophobic ligand preferably has at least one selected from a group consisting of phenyl, n-butyl, n-hexyl, n-octyl, and n-octadecyl.

A particulate plug for removing a preservative from a solution, suspension, or emulsion comprising a drug is presented. The plug comprises microparticles of a hydrophobic polymer/fatty acid blend. The microparticles of hydrophobic polymer/fatty acid blend selectively absorb preservative allowing the drug to remain in solution for delivery.

The present invention is related a method of purifying a heterologous protein from an egg white. In some embodiments, the disclosure is directed to a method of purifying a heterologous protein from an egg white comprising the heterologous protein, the method comprising, (a) adjusting the pH of the egg white to a pH of 5.8 to 6.5 to form a pH-adjusted egg white; (b) filtering the pH-adjusted egg white of (a) and collecting a first filtrate; (c) subjecting the first filtrate of (b) to a hydrophobic interaction chromatography matrix, and collecting a first eluate comprising the heterologous protein; (d) adjusting the pH of the first eluate of (c) to a pH of 5.0 to 5.6 to form a pH-adjusted eluate; (e) filtering the pH-adjusted eluate to obtain a second filtrate; (f) adjusting the pH of the second filtrate to a pH of 3.0 to 4.0 to form a pH-adjusted second filtrate; (g) neutralizing the pH-adjusted second filtrate of (f) to a pH of 5.0 to 8.0 to form a neutralized solution; (h) subjecting the neutralized solution to a cation exchange chromatography matrix and collecting a second eluate comprising the heterologous protein.

The present invention relates to the process to prepare recombinant lectin having amino acid sequence of SEQ ID NO:1, wherein the process comprises fed-batch fermentation of a clone in a host cell at specific feeding rate with carbon to Nitrogen ratio of 3:1 to 6:1. The invention also relates to the process of purification of recombinant lectin having amino acid sequence of SEQ ID NO: 1.

A purification agent which includes a compound having a betaine structure, and which is for a sugar chain having a length equal to or longer than that of a monosaccharide or for a glycopeptide having a sugar chain having a length equal to or longer than that of a monosaccharide.

Disclosed are methods for the production and/or purification of a recombinant AAV (rAAV) particle from a mammalian host cell culture.

Disclosed are methods for the production and/or purification of a recombinant AAV (rAAV) particle from a mammalian host cell culture.

Provided herein are methods of reducing bioburden of (e.g., sterilizing) a chromatography resin that include exposing a container including a composition including a chromatography resin and at least one antioxidant agent and/or chelator to a dose of gamma-irradiation sufficient to reduce the bioburden of the container and the chromatography resin, where the at least one antioxidant agent and/or chelator are present in an amount sufficient to ameliorate the loss of binding capacity of the chromatography resin after/upon exposure to the dose of gamma-irradiation. Also provided are reduced bioburden chromatography columns including the reduced bioburden chromatography resin, compositions including a chromatography resin and at least one chelator and/or antioxidant agent, methods of performing reduced bioburden column chromatography using one of these reduced bioburden chromatography columns, and integrated, closed, and continuous processes for reduced bioburden manufacturing of a purified recombinant protein.

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 nm alone on HIC-HPLC elutes at distinct run time with little overlap from the other antibody molecules in the mixture, or both.

Methods for the production of high purity recombinant protein such as monoclonal antibodies (mAb) using disulfide bond re-oxidation are provided. In particular, the present disclosure provides methods for converting partial molecules (e.g., antibody fragments) to full molecules (e.g., full antibodies) comprising admixing a starting solution comprising the partial molecules with a redox buffer comprising a redox pair which comprises at least one thiol reducing agent (e.g., cysteine) and at least one thiol oxidizing agent (e.g., cystine), wherein the redox buffer re-oxidizes the partial molecules to full molecules. The disclosed methods can be used, e.g., to prevent or mitigate the formation of partial molecules during protein purification, or to reprocess or rescue a solution comprising partial molecules (e.g., a partially degraded pharmaceutical formulation).