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FEBS Lett. 2014 Jan 21;588(2):236-46. doi: 10.1016/j.febslet.2013.10.044. Epub 2013 Nov 6.

Production of prone-to-aggregate proteins.

Author information

1
Protein Expression and Purification Facilities, Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem, Israel. Electronic address: mario.l@mail.huji.ac.il.
2
Protein Expression and Purification Facilities, Wolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem, Israel.

Abstract

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.

KEYWORDS:

Aggregation analysis; Aggregation suppressor; Buffer condition; Chaotrope; Chaperone; Fusion protein; Induction condition; Intrinsically disordered protein; Intrinsically disordered region; Kosmotrope; Protein aggregation; Protein concentration; Protein storage; Stabilizer

PMID:
24211444
DOI:
10.1016/j.febslet.2013.10.044
[Indexed for MEDLINE]
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