中文摘要：

采用PCR技术扩增TAT—H1bs融合基因，并通过基因操作构建了融合基因的原核重组载体pET-28a—TAT-H1hs。将阳性重组质粒转化至受体菌Rosseta（DE3）感受态细胞中，以IPTG诱导表达，表达产物经聚丙烯酰胺凝胶电泳检测和western-hlot检测。结果表明：重组菌能够表达目的蛋白，软件分析结果表明表达蛋白约占菌体蛋白的40％，上清表达量约为20％。上清蛋白经纯化后，Western—blot结果显示，His—Tag单克隆抗体可以很好地与所表达的蛋白带特异性结合。所获得的融合蛋白以高效胞质可溶形式表达。

英文摘要：

TAT-Hlbs fusion gene was obtained through PCR amplification, and recombinant expression plasmid pET-28a-TAT-Hlbs was constructed by gene operation technology. The correct recombinant expression plasmid was transformed into the host strain Rosseta induced by IPTG. The specific protein expressed was detected by SDS- PAGE and Western blot. The result showed that the targeted protein was detected in Rosscta（DE3）, the fusion protein was expressed at high level amounting to 40% of the total bacterial protein analyzed by computer software. The amount in supernatant is about 20% . After the supernatant protein was purified, Western blot showed the monoclonal antibody anti-His-Tag could react to the targeted protein expressed specifically. The fusion protein was expressed highly in cytoplasmic fraction in Rosscta（DE3） .