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 peptide in 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.