Purification of human TRAIL extracellular region and its activity / 中国免疫学杂志

ABSTRACT

Objective:To express hTRAIL_ 41～281 protein using E.coli and refold it into a functional form.Methods:The expression of protein was induced by IPTG,protein was purified by Ni-NTA chromatography column,and refolded by dialysis ,protein purified was determined by SDS-PAGE and Western blot.Antitumor activity of hTRAIL_ 41～281 protein was measured by DNA fragmentation electropherogram.Results:Results of SDS-PAGE and Western blot proved that the 30.5 kD protein purified were hTRAIL_ 41～281 protein,the purity of protein was more than 90%.After refolding,DNA fragmentation electropherogram showed that hTRAIL_ 41～281 protein had good antitumor activity.Conclusion:hTRAIL_ 41～281 protein with antitumor activity was successfully expressed with E.coli and purified by Ni-NTA chromatography column,refolded by dialysis.