本实验截取了人降钙素受体N端胞外结构域涉及药物靶点的第20~160位氨基酸残基区域对应的编码序列,根据大肠杆菌偏爱密码子优化后,人工合成相应的基因,运用分子克隆技术将所合成的基因克隆到pET22b(+)载体,重组质粒转入大肠杆菌BL21(DE3)中原核表达.结果表明,Nt-CTR蛋白质以包涵体形式表达,所得包涵体蛋白质通过高效的复性方法,最终得到了大量纯化的可溶性Nt-CTR蛋白质.融合蛋白质通过Western-Blot鉴定表达正确.本研究为CTR的结构研究和CTR相关疾病的药物筛选提供了基础. This experiment intercepts the coding sequence corresponding to the region of amino acid residues 20 to 160 of the N-terminal extracellular domain of human calcitonin receptor involved in the drug target. According to the preference codon of Escherichia coli, the corresponding gene is artificially synthesized, The recombinant plasmid was cloned into pET22b (+) vector and the recombinant plasmid was transformed into E.coli BL21 (DE3) for prokaryotic expression.The results showed that the Nt-CTR protein was expressed as a inclusion body and the resulting inclusion protein was highly efficient And finally obtained a large number of purified soluble Nt-CTR protein.The fusion protein was identified by Western-Blot.The results provide the basis for the structural study of CTR and drug screening of CTR-related diseases.