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Production of Recombinant Chemokines and Validation of Refolding. Methods Enzymol 2016;570:539-65

Date

02/29/2016

Pubmed ID

26921961

Pubmed Central ID

PMC4811038

DOI

10.1016/bs.mie.2015.09.031

Scopus ID

2-s2.0-84959017982   10 Citations

Abstract

The diverse roles of chemokines in normal immune function and many human diseases have motivated numerous investigations into the structure and function of this family of proteins. Recombinant chemokines are often used to study how chemokines coordinate the trafficking of immune cells in various biological contexts. A reliable source of biologically active protein is vital for any in vitro or in vivo functional analysis. In this chapter, we describe a general method for the production of recombinant chemokines and robust techniques for efficient refolding that ensure consistently high biological activity. Considerations for initiating development of protocols consistent with Current Good Manufacturing Practices (cGMPs) to produce biologically active chemokines suitable for use in clinical trials are also discussed.

Author List

Veldkamp CT, Koplinski CA, Jensen DR, Peterson FC, Smits KM, Smith BL, Johnson SK, Lettieri C, Buchholz WG, Solheim JC, Volkman BF

Authors

Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Chemotaxis
Chromatography, Affinity
Chromatography, High Pressure Liquid
Cyclic GMP
Disulfides
Escherichia coli
Nuclear Magnetic Resonance, Biomolecular
Protein Engineering
Protein Processing, Post-Translational
Protein Refolding
Recombinant Proteins
Reproducibility of Results
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46