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

Int J Biol Macromol.. 2009-07;  45(1):1-7
Wu Y, Guo JF. Institute of Bioengineering, Zhejiang Sci-Tech University, Hangzhou 310018, PR China
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摘要

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.

关键词

2-SH2 protein domain; Expression and purification; NMR
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