%0 Journal Article
%T Cloning and expression of a single human immunoglobulin heavy-chain variable domain with vascular endothelial growth factor binding activity<br>一种具有人VEGF结合活性的人源单一重链可变区的克隆与表达
%A Heng Liu
%A Siguo Liu
%A Yi Wu
%A Zili M
%A Yu Liu
%A Aimin Zhang
%A Jianquan Chen
%A Guoxiang Cheng
%A <br>刘珩
%A 刘思国
%A 武艺
%A 马梓力
%A 刘煜
%A 张爱民
%A 陈建泉
%A 成国祥
%J 生物工程学报
%D 2010
%I 
%X In the application of therapeutic antibodies, large molecular weight of antibodies is always a problem that prevents them from penetrating into tissues or binding to antigenic determinants. To overcome this problem, we investigated the function of the heavy chain variable domain of a monoclonal anti-VEGF human IgM antibody derived from the Five-Feature Translocus Mice. We cloned the cDNA of the heavy chain variable domain, which was then inserted into pET28a vector and expressed in Escherichia coli. After purification and renaturation of the denatured recombinant protein, we obtained a 16 kDa antibody fragment, which is named as rhVVH. By immunoassaying its VEGF-binding capability in vitro, we proved that rhVVH retains this activity as the complete IgM. Importantly, rhVVH is shown to inhibit the HUVEC cell proliferation in a concentration-dependent manner. Our results indicate that the single heavy chain variable domain might inherit part of the biological function of the complete IgM antibody, which provided a valuable potential in further research on antibody miniaturisation.
%K human antibody
%K vascular endothelial growth factor
%K sdAbs
%K heavy-chain antibody<br>全人抗体，VEGF，单域抗体，重链抗体
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=0FD52879695C10A87C8DC54821604EEA&yid=140ECF96957D60B2&vid=96C778EE049EE47D&iid=708DD6B15D2464E8&sid=43797DD45B2BF7AC&eid=3263523096AC9895&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=0