Expression, purification and biological activities assay of human C1q and tumor necrosis factor related protein-6
10.3969/j.issn.1001-1978.2015.08.027
- VernacularTitle:人C1 q/TNFα相关蛋白-6的表达、纯化及生物活性分析
- Author:
Hongbo LI
;
Xuefei GAO
;
Na LI
;
Donghai WU
- Publication Type:Journal Article
- Keywords:
C1 q and tumor necrosis factor related pro-tein-6;
Escherichia coli;
recombinant protein;
affinity purification;
Western blot;
gel filtration chromatogra-phy
- From:
Chinese Pharmacological Bulletin
2015;(8):1165-1168
- CountryChina
- Language:Chinese
-
Abstract:
Aim To prepare soluble human C1 q and tumor necrosis factor related protein-6 in Escherichia coli and analyze the bioactivity. Methods Recombi-nant plasmid was transformed into E. coli expression strain, and the recombinant protein Trx-hCTRP6 was expressed induced by IPTG and then purified. Results Trx-hCTRP6 was expressed efficiently and purified using Ni-NTA affinity chromatography and Superdex G-75 column. The purified Trx-hCTRP6 was shown to be active under in vivo and in vitro assay conditions. Con-clusion Active Trx-hCTRP6 is efficiently prepared from E. coli protein expression system.
