- Volume 56 Issue 5
DOI QR Code
Expression and Purification of Recombinant Human Epidermal Growth Factor Using Fusion Partners in Escherichia coli
융합 파트너를 이용한 인간 상피세포성장인자의 재조합 대장균에서 발현과 정제 연구
- Sung, Keehyun (Department of Chemical Engineering and Applied Chemistry, Chungnam National University) ;
- Kim, In Ho (Department of Chemical Engineering and Applied Chemistry, Chungnam National University)
- Received : 2018.07.04
- Accepted : 2018.08.14
- Published : 2018.10.01
Human epidermal growth factor (hEGF) can stimulate the division of various cell types and has potential clinical applications. Since the protein contains three intra-molecular disulfide bonds, the high expression of active hEGF in Escherichia coli has not been well researched, We fused the hEGF gene with a small ubiquitin-related modifier gene (SUMO) by synthesizing an artificial SUMO-hEGF fusion gene that was highly expressed in E. coli (DE3) strain. The optimal expression level of the soluble fusion protein, SUMO-hEGF with IPTG (Isopropyl-
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