Phospho-SHP-1 (Tyr564) (D11G5) Rabbit mAbProduct information
|100 µl (10 western blots)||-||Unavailable in your region|
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|
|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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