Journal
FEBS LETTERS
Volume 588, Issue 2, Pages 236-246Publisher
WILEY
DOI: 10.1016/j.febslet.2013.10.044
Keywords
Intrinsically disordered protein; Intrinsically disordered region; Induction condition; Fusion protein; Chaperone; Protein aggregation; Protein storage; Protein concentration; Stabilizer; Aggregation suppressor; Chaotrope; Kosmotrope; Buffer condition; Aggregation analysis
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Expression of recombinant proteins in Escherichia coli ( E. coli) remains the most popular and cost-effective method for producing proteins in basic research and for pharmaceutical applications. Despite accumulating experience and methodologies developed over the years, production of recombinant proteins prone to aggregate in E. coli-based systems poses a major challenge in most research applications. The challenge of manufacturing these proteins for pharmaceutical applications is even greater. This review will discuss effective methods to reduce and even prevent the formation of aggregates in the course of recombinant protein production. We will focus on important steps along the production path, which include cloning, expression, purification, concentration, and storage. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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