| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1987810 | International Journal of Biological Macromolecules | 2009 | 7 Pages |
Abstract
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.
Keywords
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Biochemistry
Authors
Ye Wu, Jiang-Feng Guo,