摘要
采用生物工程的手段,用插有食管癌相关基因2(ECRG2)开放阅读框(ORF)的原核表达质粒pEGX-4T-1转化大肠杆菌E.coli,诱导表达了重组的GST-ECRG2融合蛋白;收集GST-ECRG2融合蛋白包涵体,经SKL溶解后在PBS中透析复性,用GST亲和层析柱纯化,从而获得一定数量的高纯度重组ECRG2蛋白.
In this study, ORF of ECRG2 cDNA was cloned into the pEGX-4T-1 vector and expressed in Eseheriehia eoli as a GST fusion protein. Inclusion body GST-ECRG2 was collected, dissolved in SKL, refolded in PBS and purified using GST affinity column. After optimization,purified protein has been obtained at high yield.
出处
《汕头大学学报（自然科学版）》
2006年第2期29-32,48,共5页
Journal of Shantou University：Natural Science Edition
基金
国家基础研究重点资助项目973(No:2004CB518701)
汕头大学博士后启动基金资助项目(No:L05005)
关键词
ECRG2
包涵体
纯化
ECRG2
inclusion body
purification
