Objective:To obtain human S100A6-GST fusion protein as material of the study of function of hS100A6.Methods:The hS100A6 gene from pHAHA-hS100A6 was subcloned into the prokaryotic GST fusion protein expression plasmid

pGST-moluc

to form pGST-moluc-hS100A6. The recombinant plasmid was transformed to E.coli BL2l and the expression of hS100A6-GST fusion protein was induced with IPTG. The protein was detected by SDS-PAGE and purified with Glutathion-Sepharose 4B beads

then identified by western blot assays. Results:A 36 000 Dalton protein

as expected

was obtained evidently.The concentration of the purified fusion protein was 3mg/L bacterial culture

and the purity was about 92%. Conclusion:A prokaryotic system expressing hS100A6-GST fusion protein was successfully constructed.hS100A6-GST fusion protein with high purity could be obtained after it was efficiently expressed in E.coli BL21 and purified with Glutathion-Sepharose 4B beads. This will facilitate our study of the function of hS100A6.