Study on the preparation of recombinant human HSP70 and its presenting-antigen function

Abstract

The preparation of recombinant human HSP70 and its presenting-antigen function were investigated. Cultured in glucose-free M9ZB medium and induced with IPTG and lactose at a final concentration of 0. 02 mmol/L and 5 mmol/L respectively, the engineered bacteria carrying expression vector of human HSP70 gene expressed rHSP70 at an efficiency of 60 %. After the purification with DEAE ion-exchange chromatography, HSP70 with a purity of higher than 90 % was obtained. The purified product could bind tumor-antigen peptidein vitro, and the binding was identified by native PAGE containing 5 % glycerol. HSP70-peptide complex could activate lymphocytes to produce specific cytotoxicity to tumor cells, suggesting that the recombinant human HSP70 could be used as an antigen-presenting reagent in tumor therapy.

Keywords

recombination / heat shock protein 70 / antigen peptide / tumor

References

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