用于NMR结构研究的SHP-2蛋白N端SH2结构域的高效率原核制备

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. Then it was introduced into E. coli BL21 (DE3) for prokaryotic expressions. The NSH2 protein was labeled with 15N isotope and purified to a high purity. 1H-15N HSQC spectrum indicated a well defined tertiary structure of the NSH2 that suitable for 3D NMR studies.