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中国农学通报 ›› 2008, Vol. 24 ›› Issue (7): 22-25.

所属专题: 生物技术

• 畜牧 动物医学 蚕 蜂 • 上一篇    下一篇

胸腺肽αl原核表达载体的构建及在大肠杆菌中的表达

崔雪志, ,马凤龙,乔彦良,刘焕奇,任庆娜,刘焕珍   

  • 收稿日期:2008-05-06 修回日期:2008-05-14 出版日期:2008-07-05 发布日期:2008-07-05

Construct Prokaryotic Expression Vector of Thymosin Alpha l and Expression in Escherichia coli

Cui Xuezhi, , Ma Fenglong, Qiao Yanliang, Liu Huanqi, Ren Qingna, Liu Huanzhen   

  • Received:2008-05-06 Revised:2008-05-14 Online:2008-07-05 Published:2008-07-05

摘要: 构建胸腺肽αl(Thymosin αl,Tαl)基因原核表达载体,并在大肠杆菌BL21中进行表达,为大量获得胸腺肽αl打下基础。将人工合成的Tαl三串体基因插入到表达载体pET32a后,CaC12法转化大肠杆菌BL21,经氨苄青霉素筛选后用IPTG诱导表达,SDS-PAGE检测BL21中胸腺肽αl的表达。大肠杆菌中检测到与目的蛋白相对分子量(31kD)相符的条带。成功构建了Tαl原核表达载体,该蛋白能在大肠杆菌中表达。

关键词: 小麦, 小麦, 水分, 品质性状, 相关性

Abstract: To construct prokaryotic expression vector of thymosin alpha l (Tαl), and express in Escherichia coli strain BL21, make foundation to gain amounts of thymosin alpha l (Tαl). The four repeats of thymosin alpha l (Tαl), which was chemically synthesized, was inserted into expression vector pET32a. The recombined pET32a-3Tαl was transferred into Escherichia coli strain BL21with CaCl2. After screening with Ampicillin, the positive clone was induced to express with IPTG, and the expression product was analyzed with SDS-PAGE. A positive protein band, which was the same as interest protein molecular weight about 31kD, was found in the expression product. The gene of Tαl was cloned into the expression vector correctly and was expressed successfully in E. coli expression system.

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