以构建的表达拟南芥热激因子HsfA1 a C端氨基酸331到氨基酸486(简称ΔHsfA1 a)的大肠杆菌E coliM15为材料,用异丙基硫代-β-D-半乳糖苷(IPTG)诱导表达ΔHsfA1 a,再通过N i-NTA-Agarose亲和层析纯化表达的ΔHsfA1 a,通过SDS-PAGE电泳分析表达蛋白和纯化蛋白,获得了表达纯化的ΔHsfA1 a.
[ Objective ] This study was to express and purify Arabidopsis thaliana heat shock factor HSF1. [ Method ] Using Escherichia coli M15 harboring HSF1 （pQE32/His6-HSF1, pREP4） as experimental materials, HSF1 was induced to express with isopropyl-β-D-galactoside （IPTG） ; then the expression product was purified using Ni-NTA-agarose affinity chromatography and analyzed by SDS-PAGE. [Result] HSF1 of Arabidopsis thaliana was successfully expressed and purified. [ Conclusion] This study provides materials for understanding the blinding site of HSF1 on Arabidopsis thaliana chromosome, further laying a good foundation for revealing the regulatory mechanism and physiological function of HSF1.
Heat shock factors (HSF) are the central regulators of heat shock response in all eukaryotes[1,2]. HSF is pres...
Lihong Guo1, Yan Yuan1, Lemin Zhang2 and Shanna Chen2* 1 Department of Life Science and Technology , Kunming University, Kunming 650031, China 2 School of Life Sciences, Yunnan University, Kunming 650091, China
