Recombinant E.Coli Chaperone S

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

Generation of Recombinant Baculovirus DNA in E.coli Using a Baculovirus Shuttle Vector

of the Autographa californica nuclear polyhedrosis virus (AcNPV) are abundantly expressed during the late stages of infection. The recombinant proteins are usually soluble and functionally similar to their authentic counterparts (l –7 ). In the following sections

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

, as well as that of most recombinant proteins, requires the assistance of folding modulators that can be broadly classified as molecular chaperones and foldases.