Product Details
| Alternative Name: | Src homology-2 containing protein tyrosine phosphatase 1 |
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| MW: | 67.5 kDa |
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| Source: | Produced in E. coli. Full length human Shp-1 (aa 1-595). |
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| UniProt ID: | P29350 |
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| Formulation: | Liquid. In 50mM TRIS/HCl, pH 8.0, containing 150mM NaCl, 5mM DTT, 0.03% Brij 35, 0.1mM EDTA and 10% glycerol. |
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| Purity: | ≥90% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Specific Activity: | ≥2000 pmol/min/µg assayed by p-nitrophenylphosphate (pNPP, 50 mM) hydrolysis at pH 7.0, 30°C |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | Shp-1 is one of two human “Src Homology-2 (SH2) containing phosphatases”, enzymes in which two regulatory phosphotyrosine binding domains (N-SH2 & C-SH2) lie N-terminal to the catalytic (PTP) domain. Recruitment of Shp-1 (Src Homology-2 (SH2) containing phosphatase-1) to cell-surface receptors is mediated by SH2-domain binding to “Immuno-receptor Tyrosine-based Inhibitory Motifs” (consensus ITIM: [I/V/L]-x-pY-x-x-[I/V/L]; death receptor variant: A-x-pY-x-x-L). This binding activates Shp-1 phosphatase by displacing an inhibitory interaction between the N-SH2 and PTP domains. By dephosphorylating the downstream elements of various signal transduction pathways, Shp-1 acts as a negative regulator. Shp-1 is highly expressed in hematopoietic cells and to a lesser extent in epithelial cells. It plays a significant role in various stages of hematopoietic development and in limiting neutrophil activation and inflammatory tissue damage through down-regulation of anti-apoptotic, cytokine-derived signals. In most lymphomas and leukemias Shp-1 expression is decreased or absent and Shp-1 may play a role in the pathogenesis of these and other cancers. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE analysis: Lane 1: MW Marker; Lane 2: 2.0μg of purified Shp-1 (human) (recombinant).
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Product Literature References
The myeloperoxidase-derived oxidant hypothiocyanous acid inhibits protein tyrosine phosphatases via oxidation of key cysteine residues: N.L. Cook, et al.; Free Radic. Biol. Med.
90, 195 (2016),
Abstract;
Syntheses and activities of backbone-side chain cyclic octapeptide ligands with N-functionalized phosphotyrosine for the N-terminal SH2-domain of the protein tyrosine phosphatase SHP-1: M.S. Zoda, et al.; J. Pept. Sci.
16, 403 (2010),
Abstract;
