Literature DB >> 17536514

[Recombinant protein production in Escherichia coli].

Przemysław Nuc1, Katarzyna Nuc.   

Abstract

Growing needs for efficient recombinant production pose new challenges; starting from cell growth optimization under overexpression conditions, improving vectors, gene and protein sequence to suit them to protein biosynthesis machinery of the host, through extending the knowledge of protein folding, fusion protein construction, and coexpression systems, to improvements in protein purification and renaturation technologies. Hitherto Escherichia coli is the most defined and the cheapest protein biosynthesis system. With its wealth of available mutants tested is the best suited to economically test new gene constructs and to scale up the recombinant protein production.

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Year:  2006        PMID: 17536514

Source DB:  PubMed          Journal:  Postepy Biochem        ISSN: 0032-5422


  2 in total

1.  Cloning and expression of visfatin and screening of oligopeptides binding with visfatin.

Authors:  Xin Yu Liu; Lin Ge; De Min Yu
Journal:  Int J Clin Exp Med       Date:  2014-12-15

2.  High-efficiency expression of TAT-bFGF fusion protein in Escherichia coli and the effect on hypertrophic scar tissue.

Authors:  Xuechao Jia; Haishan Tian; Lu Tang; Long Zheng; Lulu Zheng; Ting Yang; Bingjie Yu; Zhitao Wang; Peng Lin; Xiaokun Li; Xiaojie Wang
Journal:  PLoS One       Date:  2015-02-23       Impact factor: 3.240

  2 in total

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