用于NMR结构研究的SHP-2蛋白N端SH2结构域的原核制备[EB/OL]
北京：中国科技论文在线
SHP-2的N端SH2结构域是细胞因子或病毒因子激活该蛋白的分子内靶点
下一步将用于NSH2蛋白与CagA蛋白的滴定NMR结构研究
设计引物通过PCR克隆出人SHP-2蛋白N端SH2结构域（NSH2）的DNA序列
） 摘要： SHP-2蛋白是一种含有两个SH2结构域的磷酸酶
之后浓缩达到了NMR结构研究实验的要求
） Abstract： SHP-2 protein, which has two SH2 domains, is essential for the embryonic development, haematopoiesis and signaling downstream of a variety of growth factors
SHP-2 proteins are related to many diseases
To facilitate fundamental studies, it is important that the proteins can be expressed in high quality and in a large quantity
In this work, the amino-terminal SH2 (NSH2) domain of SHP-2 protein which is important for the protein’s self-regulation was recombinated into the prokaryotic expression vector, pGEX-2T, and introduced into E
coli BL21 (DE3) for a prokaryotic expression
The NSH2 protein was labeled with 15N isotope and purified to a high purity
It would be titration with CagA Phosphopeptides for NMR studies
Keywords： SHP-2; SH2; Protein solubility; Protein stability; NMR 下载PDF阅读器 PDF全文下载： 初稿 （ 211 ） 作者简介： 通信联系人： 【收录情况】 中国科技论文在线： 牛皋
以从分子结构水平上揭示CagA蛋白的致病机理
【详情见下载】
