真姬菇热激蛋白70（HmHSP70）的纯化

SDS-PAGE analysis revealed that different concentration gradient of IPTG was set to induce and obtained with the recombinant plasmid pET32a-c(+)/HmHSP70 E.coli, which produced soluble recombinant protein. When the final inducing concentration of IPTG was 0.15 mmol/L, The amount of Soluble recombinant protein was highest and the concentration of recombinant protein was 22.5mg/ml. At the same time, the result of SDS-PAGE was indicated that the predicted molecular weight of recombinant protein was 90KDa .After the inclusion bodies was denatured and renatured, it became soluble protein; Through the Ni-affinity chromatography and the effection of enterokinase, HmHSP70 was obtained in high purity, the molecular weight of the expressed protein is 70KDa, the same as the expected result.