High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli |
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| Authors: | Huiyan Wang Yechen Xiao Lianjun Fu Hongxin Zhao Yaofang Zhang Xiaoshan Wan Yuxia Qin Yadong Huang Hongchang Gao Xiaokun Li |
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| Affiliation: | (1) Engineering Research Center of Bioreactor and Pharmaceutical Development, Ministry of Education, Jilin Agricultural University, 130118, China;(2) School of Pharmacy, Wenzhou Medical College, 325000 Wenzhou, Zhejiang, China;(3) Jilin Agricultural Science and Technology College, 132101, China;(4) Biopharmaceutical research and Development Center, Institute of Life and Health Engineering, Jinan University, 510642 Guangzhou, China |
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| Abstract: | Background Fibroblast growth factor 21 (FGF21) is a promising drug candidate to combat metabolic diseases. However, high-level expression and purification of recombinant FGF21 (rFGF21) in Escherichia coli (E. coli) is difficult because rFGF21 forms inclusion bodies in the bacteria making it difficult to purify and obtain high concentrations of bioactive rFGF21. To overcome this problem, we fused the FGF21 with SUMO (Small ubiquitin-related modifier) by polymerase chain reaction (PCR), and expressed the fused gene in E. coli BL21(DE3). |
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