目的　原核表达HES1分子 ,并制备其特异性多克隆抗体 ,以研究该分子在肿瘤细胞中的表达情况。方法　诱导表达GST HES1融合蛋白和GST ,经谷胱甘肽 Sepharose 4B亲和纯化后 ,用GST偶联预激活的Sepharose 4B ,以GST HES1为免疫原制备兔抗血清。得到的抗血清经GST Sepharose 4B吸收抗GST成分 ,以间接ELISA和Westernblot鉴定抗体特异性 ,以Westernblot分析胃癌、结肠癌及其相应非癌变组织中HES1的表达水平。结果　成功地表达并纯化了GST HES1融合蛋白。制备的抗HES1多克隆抗体具有很高的特异性 ,与GST或大肠杆菌成分无交叉反应 ,用于进行天然HES1分子的Westernblot检测时效果良好。初步检测发现 ,胃癌和结肠癌中HES1的表达水平明显高于相应的正常组织。结论　通过原核表达并纯化HES1,成功地制备了该分子的特异性多克隆抗体 ,初步应用效果满意 Objective To express HES1 gene in prokaryotic cells and prepare its specific polyclonal antibody to study the expression of HES1 in tumor cells. Methods The GST HES1 fusion protein and GST were induced and expressed. After affinity purification with glutathione Sepharose 4B, rabbit antisera were prepared by GST coupled preactivated Sepharose 4B and GST HES1 as the immunogen. The obtained antisera was absorbed on GST by GST Sepharose 4B, antibody specificity was detected by indirect ELISA and Western blot, and the expression of HES1 in gastric cancer, colon cancer and corresponding non-cancerous tissues was analyzed by Western blot. Results The GST HES1 fusion protein was successfully expressed and purified. The prepared anti-HES1 polyclonal antibody has high specificity and does not cross-react with GST or E. coli components and is used for performing western blot detection of native HES1 molecules. Preliminary testing found that gastric cancer and colon cancer HES1 expression was significantly higher than the corresponding normal tissue. Conclusion The specific polyclonal antibody of this molecule was successfully prepared by prokaryotic expression and purification of HES1, and the preliminary application results were satisfactory