%0 Journal Article
%T Porcine Follistatin cDNA Cloning and Expression in Escherichia coli<br>猪Follistatin cDNA克隆及在大肠杆菌中的表达
%A HE Xin
%A QI Bing
%A HE Li-Qian
%A CHEN Yong-Fu
%A LIU Gui-Sheng
%A CHEN Qing-Xuan
%A <br>何新
%A 齐冰
%A 何立千
%A 陈永福
%A 刘桂生
%A 陈清轩
%J 生物工程学报
%D 2006
%I 
%X The total RNA was extracted from porcine ovary. Porcine Follistatin cDNA was cloned by RT-PCR. Complete porcine follistatin cDNA coding sequences are presented including 1038 bp of open reading frame. The purified porcine follistatin cDNA was inserted into pGEX-4T-3 vector to construct the prokaryotic fusion protein expression vector. The recombinant expression plasmid was transformed into BL21 (DE3) and expression was induced by IPTG. Protein products were detected by SDS-PAGE and confirmed by Western blotting analysis, which showed that the yield of the Follistatin cDNA was a 63kD protein expression vector. Follistatin protein was expressed in the form of glutathione-S-transferase (GST) fusion protein in E. coli.
%K RT-PCR
%K porcine follistatin cDNA
%K prokaryotes expression<br>RT-PCR
%K 猪Follistatin
%K cDNA
%K 原核表达
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=2BD5D5A501FF26AB&yid=37904DC365DD7266&vid=BC12EA701C895178&iid=E158A972A605785F&sid=2E4E3741E8FB64E9&eid=8243B77967FFD12E&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=3&reference_num=12