%0 Journal Article
%T Expression of Goose Interleukin-2 gene in Escherichia coli and Isolation of Its Soluble Monomer<br>鹅IL-2基因在大肠杆菌中的表达及其可溶性单体的分离
%A Jing Qi
%A Jigang Chen
%A Jinyong Wang
%A Jie Fang
%A Jiajun Wu
%A Jiyong Zhou
%A <br>齐 静
%A 陈吉刚
%A 王金勇
%A 方 杰
%A 吴佳俊
%A 周继勇
%J 生物工程学报
%D 2008
%I 
%X Recombinant expression plasmid of pET-28a (+)-goIL-2 was constructed by inserting the goose IL-2 gene without the signal peptide sequence into the prokaryotic expression vector pET-28a (+), and transformed into the bacterial competent E. coli BL21 (DE3) cells for expression. After IPTG induction, an expected protein band with molecular weight of 15.0 kD was observed on SDS-PAGE gel, recognized by monoclonal antibody against goose IL-2 in western-blotting assay. In the pET-28a (+) expression system, much of the recombinant goose IL-2 (rgoIL-2) was found in inclusion bodies with a portion of soluble protein. The monomer and multimers of soluble goose interleukin 2 proteins were observed in native electrophoresis. The rgoIL-2 proteins were purified by Ni-NTA column under a native condition. The rgoIL-2 soluble protein monomer was isolated by a quick protein isolation and purification system of ?KTA FPLC and identified by native PAGE. Bioactivity analysis showed that the rgoIL-2 monomer stimulated the proliferation of goose lymphocytes in vitro. This will establish a basis for further study about the biological function and clinical application of goose IL-2.
%K goose interleukin 2
%K prokaryotic expression
%K purification
%K monomer<br>鹅IL-2
%K 原核表达
%K 纯化
%K 单体
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=77BC6202D07D274CF30FF5988DFE0047&yid=67289AFF6305E306&vid=B91E8C6D6FE990DB&iid=0B39A22176CE99FB&sid=DD74772618543076&eid=3E0812ED84A7B31D&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=11