摘要
以PET30a为载体构建的表达拟南芥热激因子AtHsfA1a的大肠杆菌E coli M15(pET30a/His6-AtHsfA1a)为实验材料,以IPTG诱导6×His融合蛋白的表达并经过Ni2+柱分离纯化AtHsfA1a,再通过SDS-PAGE鉴定表达蛋白和纯化蛋白.结果显示,AtHsfA1a蛋白在在PET原核表达系统中能够有效表达,并能通过亲和层析获得纯化的AtHsfA1a蛋白.研究结果为揭示拟南芥热激因子AtHsfA1a的作用机理奠定基础.
E coli M15 （ （pET30a His6-AtAtHsfAla） was used as experimental materials. Expression of AtHsfA1 a in Arabidopsis thaliana was induced with isopropyl-13-D-galactoside （IPTG）. AtHsfAla was purified by the Ni-NTA-Agarose affinity chromatography. AtHsfAla was analyzed by the SDS-PAGE eleetrophoresis. Heat shock factor HsfAla in Arabidopsis thaliana was expressed and purified. The result showed that experimental material was provided for isolating and identifying of heat shock elements （ HSE ） bound in vivo by heat shock factor HSF in Arabidopsis thaliana and founded the basis for the function mechanism of heat shock factor AtHsfAla.
出处
《昆明学院学报》
2011年第6期75-76,84,共3页
Journal of Kunming University
基金
国家自然科学基金资助项目(31060039)
云南省自然科学基金资助项目(2010ZC163)
昆明学院科学研究资助项目(YJL11025)
校级重点学科建设
