anti-SHP2, mAb (5F2)

CHF 322.00
In stock
YIF-LF-MA0186100 µlCHF 322.00
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Product Details
Synonyms Shp2; PTP2C; SHP-2; PTP-2C; PTP-1D; PTPN11; SH-PTP3; SH-PTP2; EC=3.1.3.48; Protein-Tyrosine Phosphatase 1D; Protein-Tyrosine Phosphatase 2C; Tyrosine-Protein Phosphatase Non-Receptor Type 11
Product Type Monoclonal Antibody
Properties
Clone 5F2
Isotype Mouse IgG1 κ
Immunogen/Antigen Recombinant human GST-SHP2 protein purified from E. coli.
Application

Western Blot (1:2,000)
Immunoprecipitation (1 μl)

Crossreactivity Human
Mouse
Rat
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

SHP2 is a tyrosine phosphatase containing two tandem SH2 (src homology 2) domains. Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Together with tyrosine kinases, PTPs regulate the phosphorylation state of many important signaling molecules. SHP1 and SHP2 represent a subfamily of non-transmembrane PTPs that contain two SH2 domains followed by a PTP domain. Tyrosine phosphorylation of SHP2 is required for normal ERK activation in response to some growth factors. In the inactive state, the N-terminal SH2 domain binds the PTP domain and blocks access of potential substrates to the active site. This auto-inhibition is relieved by the binding of phosphopeptides to SH2 domain, resulting in activation of phostphatase activity. Noonan syndrome characterized by an abnormal face, short stature and cardiac abnormalities is due to the mutations of N-terminal SH2 domain or PTP domain. SHP2 mutations might also cause some leukemia, and could be important in pathogenesis by Helicobacter pylori, the major cause of gastric ulcer and carcinoma. Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus.

Product References

1) Salmond R.J. and Alexander D.R., (2006) Trends Immunol. 27:154-160. (General)
2) Neel B.G. et al., (2003) Trends Biochem Sci. 28:284-293. (General)
3) Agazie M. and Hayman M.J., (2003) Mol Cell Biol. 23:7875-7886. (General)
4) Araki T. et al., (2003) J Biol Chem. 278:41677-41684. (General)
5) Yu D.H. et al., (1998) J Biol Chem. 273:21125-21131. (General)

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