Recombinant Human Active SHP-2 Protein, CF

Src-Homology domain-2 containing protein tyrosine Phosphatase 2 (SHP-2), also called protein tyrosine phosphatase, non-receptor type 11 (PTPN11), PTP1D, PTP2C, and SYP, is an enzyme that dephosphorylates tyrosine residues in proteins. The protein contains two Src homology 2 (SH2) domains, which both regulate the activity of the enzyme (1) and allow it to selectively bind to SH2 sites on proteins such as Dok1, IRS1, and the insulin receptor (2). SHP-2 plays a unique stimulatory role in cell signaling. Cells lacking SHP-2 have poor mobility because the hyper-phosphorylation of FAK and other proteins in the focal adhesion complex (3) prevents turnover of cellular attachment points. Without SHP-2, sustained ERK stimulation does not take place (4). The Y992 phosphorylation site of EGFR is a particularly good substrate for SHP-2 (5) and a phosphopeptide containing this sequence can be used to measure the activity of the enzyme (Catalog # http://www.rndsystems.com/product_results.aspx?k=ES006">ES006) by detecting release of phosphate (Catalog # http://www.rndsystems.com/product_results.aspx?k=DY996">DY996).