Research Progress Fusion Tags for Recombinant Protein Production.

IF 3.2 4区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Jing-Jia Yuan, Shao-Lei Geng, Tian-Yun Wang
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引用次数: 0

Abstract

Recombinant proteins are obtained using genetic engineering techniques and are widely used in various fields. Some recombinant proteins are difficult to express, purify, or are unstable or insoluble due to their structural characteristics. In order to address such issues, additional tags are fused at either the N- or C-terminal end of the protein of interest during the cloning procedure. These tags range from a few residues to full-length proteins or domains not only maintaining the structure of the natural protein but can be used to improve the solubility, stability, yield, or to confer new properties of the target protein. Here, the fusion tags commonly used in recombinant protein production and their functions are reviewed, and novel fusion tags are also summarized.

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来源期刊
Biotechnology and applied biochemistry
Biotechnology and applied biochemistry 工程技术-生化与分子生物学
CiteScore
6.00
自引率
7.10%
发文量
117
审稿时长
3 months
期刊介绍: Published since 1979, Biotechnology and Applied Biochemistry is dedicated to the rapid publication of high quality, significant research at the interface between life sciences and their technological exploitation. The Editors will consider papers for publication based on their novelty and impact as well as their contribution to the advancement of medical biotechnology and industrial biotechnology, covering cutting-edge research in synthetic biology, systems biology, metabolic engineering, bioengineering, biomaterials, biosensing, and nano-biotechnology.
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