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HCP; PTPN6; PTP-1C; SH-PTP1; EC=3.1.3.48; Protein-Tyrosine Phosphatase 1C; Protein-Tyrosine Phosphatase SHP-1; Hematopoietic Cell Protein-Tyrosine Phosphatase; Tyrosine-Protein Phosphatase Non-Receptor Type 6

Monoclonal Antibody

10F5

Mouse IgG1 κ

Recombinant human His/ABD-SHP1 protein purified from E. coli.

ELISAWestern Blot (1:2,000)

Human

Ammonium sulfate precipitation.

Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.

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

Manufactured by AbFrontier

BLUE ICE

+4°C

-20°C

Stable for at least 1 year after receipt when stored at -20°C.

No

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SHP1 and SHP2 represent a subfamily of non-transmembrane protein-tyrosine phosphatases (PTPs) that contain two tandem SH2 (src homology 2) domains. SHPs have two N-terminal SH2 domains (N-SH2 and C-SH2), a classic PTP domain and a C-terminal tail harboring two tyrosyl phosphorylation sites which are phosphorylated differentially by receptor and non-receptor protein-tyrosine kinases (PTKs). Whereas SHP2 is expressed ubiquitously, SHP1 is primarily expressed in hematopoietic cells and behaves as a key regulator controlling intracellular phosphotyrosine levels in lymphocytes. SH2 domains (particularly the N-SH2) also regulate PTP activity. Basal SHP activity is low, but addition of a phosphotyrosyl peptide that binds the N-SH2 (Tyr–P peptide ligand) markedly stimulates catalysis. SHP1 is implicated in signaling from receptor tyrosine kinases (RTKs), cytokine receptors, chemokine receptors and integrins. SHP1-deficient bone marrow macrophages are hyper-adherent to β1- and β2-integrin ligands. Decreased SHP1 level causes abnormal T-lymphocyte proliferation and induces various types of leukemias. Introduction of the SHP1 gene back into a leukemia cell line and a prostate cancer cell line demonstrated the tumor suppressor function of SHP1. Plays a key role in hematopoiesis. This PTPase activity may directly link growth factor receptors and other signaling proteins through protein-tyrosine phosphorylation. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation.Product References1) Honorat JF et al., (2006) Blood.107(10):4130-4138. (General)2) Neel BG et al., (2003) Trends Biochem Sci. 28:284-293. (General)3) Wu C et al.. (2003) Gene. 306:1-12. (General)