Expression of recombinant hARRG cDNA in E.coli and purification of hARRG protein

Objective To construct expression vector of the recombinant human arsenic resistance related gene (hARRG),induce its expression in DE\-3 and isolate and purify expression product,for studying the physiochemistry characteristic,function and immune activity of the protein,and further researching the arsenic resistant effects of human.Methods hARRG cDNA was subcloned into prokaryotic expression vector Pet11C.The recombinant protein expression was induced by IPTG,then,the protein was purified by anions Ion-exchange column Sepharose and examined by SDS-PAGE gel.Results hARRG cDNA was successfully subcloned into prokaryotic expression vector Pet11C and expressed in E.coli and the protein was purified by anions Ion-exchange column successfully.Conclusion Pet11C excpression vector containing hARRG cDNA wassuccessfully constructed,the cell DE\-3 transformed with expression vector capable of expression the gene and a hARRG protein could be purified by anions Ion-exchange column Sepharose.