【摘要】 水稻SDG723蛋白含有植物组蛋白甲基转移酶保守的SET结构域。选取其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-723C,转化E.coli BL21(DE3)感受态细胞,IPTG诱导表达融合蛋白后进行纯化。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。Western-blot分析表明,制备的多克隆抗体能有效地检测抗原的表达,为进一步深入研究SDG723蛋白的功能奠定了基础。更多还原

【Abstract】 Rice SDG723 contained SET domain,which was conserved in plant histone methyltransferase.In this studies,the prokaryotic expression vector of SDG723 C terminal(pET28a-723C) was constructed,and the recombinant plasmid was transformed into E.coli BL21(DE3) and the expression of recombinant protein was induced by IPTG.After purification,it was used as the antigen to immune a rabbit and then polyclonal antibody was obtained.Western-blot analysis confirmed that the polyclonal antibody was able to recognize the antigen,which was expressed in E.coli.This work laid a foundation for functional studies of SDG723.更多还原