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《China Biotechnology》 2009-08
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Expression and Characterization of a Novel Truncated TGF-β Receptor Ⅱ in Escherichia coli

CHU Yan-hui1,2 LIU Hai-feng1 WANG Xiao-hua3 ZHANG Yu-fei1 WU Yan1 YUAN Xiao-huan1(1 Heilongjiang Key Laboratory of Anti-fibrosis Biotherapy,Mu Dan Jiang Medical University,Mudanjiang 157011,China)(2 College of Life Science and Technology,Jinan University,Guangzhou 510632,China)(3 The Laboratory of Pathogeny Biology,Mu Dan Jiang Medical University,Mudanjiang 157011,China)  
To clone human truncated TGF-β receptor II(tTGF-βRII)and express it in Escherichia coli.The gene tTGF-βRIIobtained by PCR was cloned into the vector pGEX4T3 to construct a fusion expression plasmid.The recombinant protein GST-tTGF-βRII were expressed in soluble form,purified by Glutathione-Sepharose 4B affinity chromatography and cleaved by thrombin to release tTGF-βRII.Purification of tTGF-βRII was also achieved by affinity chromatography.SDS-PAGE indicated that fusion protein GST-tTGF-βRII was secreted as a protein with 37.0 kDa MW and aimed protein tTGF-βRIIwas 11.0 kDa.The GST-tTGF-βRIIand tTGF-βRII protein were confirmed by Western blot analysis.The purification of aimed protein was biologically active in a validated inhibited human fibroblast proliferation bioassay.
【Fund】: 国家“863”计划(2006AA020906);; 黑龙江省自然科学基金(D2007-99)资助项目
【CateGory Index】: Q504
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