Literature DB >> 21267760

Self-cleaving fusion tags for recombinant protein production.

Yifeng Li1.   

Abstract

Fusion expression is a common practice for recombinant protein production. Some fusion tags confer solubility on the target protein whereas others provide affinity handles that facilitate purification. However, the tag usually needs to be removed from the final product, which involves using expensive proteases or hazardous chemicals and requires additional chromatography steps. Self-cleaving tags are a special group of fusion tags that possess inducible proteolytic activity. Combined with appropriate affinity tags, they enable fusion purification, cleavage and target separation to be achieved in a single step, which saves time, labor and cost. This paper reviews currently available self-cleaving fusion tags for recombinant protein production. For each system, an introduction of its key characteristics and a brief discussion of its advantages and disadvantages is given. © Springer Science+Business Media B.V. 2011

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Year:  2011        PMID: 21267760     DOI: 10.1007/s10529-011-0533-8

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  19 in total

1.  Unprecedented rates and efficiencies revealed for new natural split inteins from metagenomic sources.

Authors:  Patricia Carvajal-Vallejos; Roser Pallissé; Henning D Mootz; Stefan R Schmidt
Journal:  J Biol Chem       Date:  2012-06-28       Impact factor: 5.157

Review 2.  Biomolecular engineering for nanobio/bionanotechnology.

Authors:  Teruyuki Nagamune
Journal:  Nano Converg       Date:  2017-04-24

3.  Purification of Antibacterial CHAPK Protein Using a Self-Cleaving Fusion Tag and Its Activity Against Methicillin-Resistant Staphylococcus aureus.

Authors:  Elahe Seyed Hosseini; Rezvan Moniri; Yasaman Dasteh Goli; Hamed Haddad Kashani
Journal:  Probiotics Antimicrob Proteins       Date:  2016-12       Impact factor: 4.609

Review 4.  An overview of enzymatic reagents for the removal of affinity tags.

Authors:  David S Waugh
Journal:  Protein Expr Purif       Date:  2011-08-19       Impact factor: 1.650

5.  Biological activities of histidine-rich peptides; merging biotechnology and nanomedicine.

Authors:  Neus Ferrer-Miralles; José Luis Corchero; Pradeep Kumar; Juan A Cedano; Kailash C Gupta; Antonio Villaverde; Esther Vazquez
Journal:  Microb Cell Fact       Date:  2011-12-02       Impact factor: 5.328

6.  Protein bodies in nature and biotechnology.

Authors:  Stefan R Schmidt
Journal:  Mol Biotechnol       Date:  2013-06       Impact factor: 2.860

Review 7.  Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system.

Authors:  Sofia Costa; André Almeida; António Castro; Lucília Domingues
Journal:  Front Microbiol       Date:  2014-02-19       Impact factor: 5.640

Review 8.  Genome engineering for improved recombinant protein expression in Escherichia coli.

Authors:  Shubhashree Mahalik; Ashish K Sharma; Krishna J Mukherjee
Journal:  Microb Cell Fact       Date:  2014-12-19       Impact factor: 5.328

Review 9.  Several affinity tags commonly used in chromatographic purification.

Authors:  Xinyu Zhao; Guoshun Li; Shufang Liang
Journal:  J Anal Methods Chem       Date:  2013-12-26       Impact factor: 2.193

10.  A new fusion protein platform for quantitatively measuring activity of multiple proteases.

Authors:  Chengdong Zhou; Yanping Yan; Jie Fang; Beijiu Cheng; Jun Fan
Journal:  Microb Cell Fact       Date:  2014-03-21       Impact factor: 5.328

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