论文部分内容阅读
[目的]对水稻SDG711蛋白C末端进行原核表达,并制备其多克隆抗体。[方法]选取水稻SDG711蛋白抗原决定簇较密集的C末端进行原核表达,通过构建原核表达载体pET28a-711C,转化E.coliBL21(DE3)感受态细胞,IPTG诱导表达融合蛋白后进行纯化,再以纯化的融合蛋白为抗原免疫新西兰白兔,制备多克隆抗体,并对其进行Western-blot分析。[结果]试验制备的多克隆抗体能有效地检测抗原的表达。[结论]该研究为进一步深入研究SDG711蛋白的功能奠定了基础。
[Objective] The prokaryotic expression of SDG711 protein in rice and its polyclonal antibody were prepared. [Method] Prokaryotic expression of rice SDG711 protein epitopes was selected. The prokaryotic expression vector pET28a-711C was constructed and transformed into E.coli BL21 (DE3) competent cells. The recombinant protein was induced by IPTG and purified by The purified fusion protein was used to immunize New Zealand white rabbits as antigens to prepare polyclonal antibodies and Western-blot analysis. [Result] The prepared polyclonal antibody could effectively detect the antigen expression. [Conclusion] This study lays a foundation for further studying the function of SDG711 protein.