Detection of Human, Mouse, and Rat SHP‑2 by Western Blot. |
Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line, TS1 mouse helper T cell line, and PC-12 rat adrenal pheochromocytoma cell line. ??? membrane was probed with 2 µg/mL Rat Anti-Human/Mouse/Rat SHP‑2 Monoclonal Antibody (Catalog # MAB1894) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). For additional reference, Recombinant Human Active SHP‑1 aa 205-595 (Catalog # 1878-SH) and Recombinant Human SHP‑2 (Catalog # 1894-SH) (2 ng/lane) were included. A specific band for SHP-2 was detected at approximately ??? kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.
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).
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