|Reactivity||Human, Mouse, Rat|
|Calculated MW||68436 Da|
|Other Names||Tyrosine-protein phosphatase non-receptor type 11, Protein-tyrosine phosphatase 1D, PTP-1D, Protein-tyrosine phosphatase 2C, PTP-2C, SH-PTP2, SHP-2, Shp2, SH-PTP3, PTPN11, PTP2C, SHPTP2|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-term of human SHP-2 was used as immunogen. This antibody is predicted to detect splice isoforms 2 and 3 based on sequence analysis.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SHP-2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73 (PubMed:26742426).|
|Cellular Location||Cytoplasm. Nucleus|
|Tissue Location||Widely expressed, with highest levels in heart, brain, and skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
SHP-2 (also called PTP2C, SH-PTP2, PTP1D, SH-PTP3, Syp and PTPN11) is a protein tyrosine phosphatase (PTP) expressed in most cell types (unlike SHP-1), (1). SHP-2 is involved in t the signal transduction stimulated by EGF, PDGF and Insulin. After cell stimulation, SHP-2 (as well as SHP-1), translocates from cytosol to the plasma membrane and binds to tyrosine-phosphorylated receptors through their SH2 domains, becoming activated in the process (2). When phosphorylated, SHP-2 has been shown to bind Grb2, EGFR, PDGFR, IRS-1 via its SH2 domain (3). Overexpression of SHP-2 leads to Juvenile Myelo-monocytic Leukemia and Noonan syndrome (4-5).
1. Ahmad, et al: Proc. Nat. Acad. Sci. 90: 2197-2201, 1993
3. Xiao et al (1994) J. Biol. Chem. 269, 21244-212484. Chen, H. E., S. Chang, T. Trub, B. G. Neel. 1996. Mol. Cell. Biol. 16:3685
4. Tartaglia et al.Hum. Genet. 70: 1555-1563, 2002.
5. Tartaglia et al. Nature Genet. 34: 148-150, 2003.
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