Expression and purification of TRAIL protein and its antitumor activity

Objective To express TRAIL protein using Escherichia coli and observe antitumor activity of purified TRAIL protein. Methods The pET d expression plasmid containing TRAIL (amino acids 114 281,with 6 his tag) gene was transfected into Escherichia coli by CaCl 2 method, the expression of protein was induced by IPTG. Protein was purified by Ni NTA chromatography column, and purified protein was determined by SDS PAGE and Western blot; Antitumor activity of TRAIL protein was measured by MTT method. Results Results of SDS PAGE and Western blot proved that the 20.1×10 3 protein purified was TRAIL protein MTT method showed that. TRAIL protein had high antitumor activity and good relationship of concentration effect and time effect. Conclusion TRAIL protein with antitumor activity was successfully expressed with Escherichia coli and purified by Ni NTA chromatography column.