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Production of prone‐to‐aggregate proteins
Author(s) -
Lebendiker Mario,
Danieli Tsafi
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.10.044
Subject(s) - recombinant dna , escherichia coli , cloning (programming) , computational biology , protein expression , aggregate (composite) , biochemical engineering , chemistry , microbiology and biotechnology , biochemistry , computer science , biology , gene , nanotechnology , engineering , materials science , programming language
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.