|Detection of Mouse Phospho-SHP‑2 (Y542) by Western Blot. Western blot shows lysates of NIH‑3T3 mouse embryonic fibroblast cell line untreated (-) or treated (+) with 50 ng/mL Human PDGF-BB (Catalog # 220-BB) for 20 minutes. PVDF membrane was probed with 1 µg/mL of Rabbit Anti-Human/Mouse Phospho-SHP‑2 (Y542) Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3790), followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for Phospho-SHP‑2 (Y542) at approximately 72 kDa (as indicated). The lysates were also probed for total SHP-2 with Human/Mouse/Rat SHP-2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1894). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Detection of Mouse Phospho-SHP‑2 (Y542) by Simple WesternTM. |
Simple Western lane view shows lysates of NIH‑3T3 mouse embryonic fibroblast cell line untreated (-) or treated (+) with 50 ng/mL Recombinant Human PDGF‑BB (Catalog # 220-BB) for 20 minutes, loaded at 0.2 mg/mL. A specific band was detected for Phospho-SHP‑2 (Y542) at approximately 72 kDa (as indicated) using 10 µg/mL of Rabbit Anti-Human/Mouse Phospho-SHP‑2 (Y542) Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3790). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
*Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.
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 (R&D Systems, Catalog # ES006) by detecting release of phosphate (R&D Systems, Catalog # DY996).
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