Expression, purification and biological activities assay of human C1q and tumor necrosis factor related protein-6 / 中国药理学通报

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.