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Shp-1 (human), (recombinant)

BML-SE334-0020 20 µg 531.00 USD
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Product Details

Alternative Name:Src homology-2 containing protein tyrosine phosphatase 1
MW:67.5 kDa
Source:Produced in E. coli. Full length human Shp-1 (aa 1-595).
UniProt ID:P29350
Formulation:Liquid. In 50mM TRIS/HCl, pH 8.0, containing 150mM NaCl, 5mM DTT, 0.03% Brij 35, 0.1mM EDTA and 10% glycerol.
Purity:≥90% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Specific Activity:≥2000 pmol/min/µg assayed by p-nitrophenylphosphate (pNPP, 50 mM) hydrolysis at pH 7.0, 30°C
Shipping:Dry Ice
Long Term Storage:-80°C
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.
Regulatory Status:RUO - Research Use Only
Shp-1 (human), (recombinant) SDS-PAGE
SDS-PAGE analysis: Lane 1: MW Marker; Lane 2: 2.0μg of purified Shp-1 (human) (recombinant).
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Shp-1 (human), (recombinant) SDS-PAGE

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;

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