Overview of fusion tags for recombinant proteins

Virtually all recombinant proteins are now prepared using fusion domains also known as “tags”. The use of tags helps to solve some serious problems: to simplify procedures of protein isolation, to increase expression and solubility of the desired protein, to simplify protein refolding and increase i...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2016-03, Vol.81 (3), p.187-200
Main Authors: Kosobokova, E. N., Skrypnik, K. A., Kosorukov, V. S.
Format: Article
Language:English
Subjects:
Affinity Labels - chemistry
Affinity Labels - metabolism
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Chromatography
Chromatography, Affinity
Escherichia coli - metabolism
Fusion
Life Sciences
Microbiology
Physiological aspects
Protein Folding
Protein Stability
Proteins
Proteolysis
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - isolation & purification
Recombinant proteins
Review
Solubility
Tags
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Summary:Virtually all recombinant proteins are now prepared using fusion domains also known as “tags”. The use of tags helps to solve some serious problems: to simplify procedures of protein isolation, to increase expression and solubility of the desired protein, to simplify protein refolding and increase its efficiency, and to prevent proteolysis. In this review, advantages and disadvantages of such fusion tags are analyzed and data on both well-known and new tags are generalized. The authors own data are also presented.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297916030019