目的　表达人热休克蛋白 70 (HSP70 )并进行鉴定。方法　用PCR方法扩增人HSP70基因片段 ,经T A克隆法克隆到载体pUCm T中 ,并进行DNA测序。将人HSP70基因片段从载体pUCm T中酶切后 ,构建重组表达载体pGEX 4T 1 HSP70 ,并转化大肠杆菌JM10 9,用IPTG诱导。收集细菌 ,菌体裂解后进行SDS PAGE及Westernblot检测。结果　人HSP70基因的PCR产物约为 1.9kb。序列测定结果证实 ,所获目的序列与文献 [3]报道的相一致。经EcoRI和XhoI酶切鉴定证实 ,人HSP70基因已成功地克隆到表达载体pGEX 4T 1中。构建的表达载体pGEX 4T 1 HSP70 ,能很好地在大肠杆菌中表达相对分子质量 (Mr)为 96 0 0 0并具有抗原特性的融合蛋白。结论　成功地克隆并表达人HSP70基因 ,为研究HSP70的结构、功能与临床应用提供了必要条件 Objective To express and identify human heat shock protein 70 (HSP70). Methods The human HSP70 gene fragment was amplified by PCR and cloned into vector pUCm T by T A cloning and sequenced. After digesting the human HSP70 gene fragment from the vector pUCm T, the recombinant expression vector pGEX 4T 1 HSP70 was constructed and transformed into E. coli JM109 and induced by IPTG. Bacteria were collected and the cells were lysed and analyzed by SDS PAGE and Western blot. Results The PCR product of human HSP70 gene was about 1.9 kb. Sequence analysis confirmed that the sequence obtained was consistent with that reported in [3]. Digestion with EcoRI and XhoI confirmed that the human HSP70 gene was successfully cloned into the expression vector pGEX 4T 1. The constructed expression vector pGEX 4T 1 HSP70 can well express the fusion protein with the molecular weight (Mr) of 96,000 and the antigenic character in E. coli. Conclusion The successful cloning and expression of human HSP70 gene provides the necessary conditions for studying the structure, function and clinical application of HSP70