摘要
目的利用大肠杆菌表达可溶性h CTRP6蛋白并分析其活性。方法重组载体转化大肠杆菌表达菌株、IPTG诱导表达、纯化后测定活性。结果 Trx-h CTRP6蛋白在大肠杆菌中高效表达,经镍亲合纯化和分子筛纯化,Trx-h CTRP6在细胞和动物水平上都有生物活性。结论利用大肠杆菌表达系统高效制备了具有生物活性的Trx-h CTRP6蛋白。
Aim To prepare soluble human C lq and tumor necrosis factor related protein-6 in Escherichia coli and analyze the bioactivity. Methods Recombi- nant plasmid was transformed into E. coli expression strain, and the recombinant protein Trx-hCTRP6 was expressed induced by IPTG and then purified. Results Trx-hCTRP6 was expressed efficiently and purified using Ni-NTA affinity chromatography and Superdex G-75 column. The purified Trx-hCTRP6 was shown to be active under in vivo and in vitro assay conditions. Con- clusion Active Trx-hCTRP6 is efficiently from E. coli protein expression system. prepared
出处
《中国药理学通报》
CAS
CSCD
北大核心
2015年第8期1165-1168,共4页
Chinese Pharmacological Bulletin
基金
国家自然科学基金资助项目(No 81300655)
湖南省重点学科建设项目(No 2011042)
广东省科技计划项目(No2013B051000090)
关键词
C1q/TNFα相关蛋白-6
大肠杆菌
重组蛋白
亲合纯化
蛋白印迹
分子筛
C1 q and tumor necrosis factor related pro-rein-6
Escherichia coli
recombinant protein
affinitypurification
Western blot
gel filtration chromatogra-phy