Product Pathways - Phosphatases
Phospho-SHP-1 (Tyr564) (D11G5) Rabbit mAb #8849
|8849S||100 µl (10 western blots)||---||In Stock||---|
|8849||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse||Endogenous||68||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-SHP-1 (Tyr564) (D11G5) Rabbit mAb recognizes endogenous levels of SHP-1 protein only when phosphorylated at Tyr564.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr564 of human SHP-1 protein.
Western blot analysis of extracts from various cell lines, untreated (-) or treated (+) with λ phosphatase, using Phospho-SHP-1 (Tyr564) (D11G5) Rabbit mAb (upper) and SHP-1 (C14H6) Rabbit mAb #3759 (lower). The JCaM1.6 cell line is a Lck kinase-deficient derivative of the Jurkat cell line. Note the corresponding reduction in phospho-SHP-1 (Tyr564) protein in JCaM1.6 cells, relative to wild-type (Jurkat) cells.
SHP-1 (PTPN6) is a non-receptor protein tyrosine phosphatase that is expressed primarily in hematopoietic cells. The enzyme is composed of two SH2 domains, a tyrosine phosphatase catalytic domain, and a carboxy-terminal regulatory domain (1). SHP-1 removes phosphates from target proteins to downregulate several tyrosine kinase-regulated pathways. In hematopoietic cells, the amino-terminal SH2 domain of SHP-1 binds to tyrosine phosphorylated erythropoietin receptors (EpoR) to negatively regulate hematopoietic growth (2). Overexpression of SHP-1 in epithelial cells results in dephosphorylation of the Ros receptor tyrosine kinase and subsequent downregulation of Ros-dependent cell proliferation and transformation (3). Following ligand binding in myeloid cells, SHP-1 associates with the IL-3R β chain and downregulates IL-3-induced tyrosine phosphorylation and cell proliferation (4). Because SHP-1 downregulates various proliferation pathways, SHP-1 is considered a potential tumor suppressor and angiogenesis regulator (5,6).
SHP-1 is a substrate of Src family kinases (7,8) and phosphorylation of Tyr564 is thought to be critical for achieving maximal phosphatase activity (8). In a murine model of chronic myelomonocytic leukemia (CMML), genetic suppression of Tyr564 phosphorylation led to constitutive overactivation of the transcription factor Stat5 and an accelerated onset of CMML-like disease (8).
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- Bhattacharya, R. et al. (2008) J Mol Signal 3, 8.
- Zhang, Z. et al. (2003) J Biol Chem 278, 4668-74.
- Xiao, W. et al. (2010) Blood 116, 6003-13.
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For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
This antibody is developed, validated, and produced by CST using in part technology under license (granting certain rights including those under U.S. Patent No. 5,675,063) from Epitomics, Inc.