Abstract: 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).

Abstract: In certain embodiments, the present invention provides a method of purifying a monomeric monoclonal antibody from a mixture which comprises the monomeric monoclonal antibody and one or more contaminants, comprising: a) subjecting the mixture to cation exchange chromatography (CEX) matrix, wherein the monomeric monoclonal antibody binds to the CEX matrix; b) contacting the CEX matrix with a wash solution at a pH which is between about 7 and about 7.8; c) eluting the monomeric monoclonal antibody from the CEX matrix into an elution solution, thereby purifying the monomeric monoclonal antibody.