Expression and purification of 15N-labeled 2-SH2 protein domain of SHP-2 from Homo sapiens in Escherichia coli for NMR studies and applications.

A method for 2-SH2 protein domain study was described as per the order of expression, purification and structural detection. The 2-SH2 protein of Homo sapiens SHP-2 was successfully expressed and purified. It could specifically bind to anti-SHP-2/SHPTP-2 antibody according to the MS and Western blot analysis. The NMR spectrum result reveals that the protein exists in a well-ordered structure. This can provide foundations to find out the reaction mechanism of the D phosphorylated-EPIYA motif accessible to 2-SH2, support the research and development of the novel detection chip as well as target inhibition medicine for the future clinical applications.