Recombinant E.Coli Chaperone P

Engineering the Chaperone Network of CHO Cells for Optimal Recombinant Protein Production and Authenticity

of proteins in both normal and stressed cells. The rational manipulation of chaperone levels in a cell line engineered to produce a defined recombinant protein (rP) can significantly improve both the achievable steady-state levels and authenticity of a wide

Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression

Protein folding in the viscous and crowded environment of the cell is very different from in vitro processes in which a single protein is allowed to refold at low concentration in an optimized buffer. Although Anfinsen's observation

Enhancing Antigen Cross-Presentation and T-Cell Priming by Complexing Protein Antigen to Recombinant Large Heat-Shock Protein

chaperone complexes of large HSPs and protein antigen may be exploited for augmentation of an antigen-specific immune response. The methods for the preparation of the recombinant protein antigen chaperone complex and characterization of its T-cell priming