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

  Objective   To construct expression vector of the recombinanthuman arsenic resistance related gene(hAR-RG), induce its expression in DE3 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-PA GE gel.

  Results   hARRGcDNA 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 DE3 transformed with expression vector capable of expression the gene and a hARRG protein could be purified by anions Ion-exchange column Sepharose.