拟南芥热激因子AtHsfA1a在PET原核表达系统中的表达及纯化  

Expression and Purification of Heat Shock Factor AtHsfA1a of Arabidopsis Thaliana in PET Expression System

作　　者：郭丽红[1] 戴利利[1] 邵春燕[1] 禹志宣[1] 

机构地区：[1]昆明学院生命科学与技术系,云南昆明650214

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

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.

关 键 词：拟南芥AtHsfAla 表达 纯化 

分 类 号：Q943.2[生物学—植物学]