Phospho-SHP-1 (Tyr564) (D11G5)

8849:

Western Blotting

Phospho-SHP-1 (Tyr564) (D11G5) Rabbit mAb recognizes endogenous levels of SHP-1 protein only when phosphorylated at Tyr564.

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr564 of human SHP-1 protein.

Western Blotting

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).

1. Yi, T.L. et al. (1992) Mol Cell Biol 12, 836-46.
2. Yi, T. et al. (1995) Blood 85, 87-95.
3. Keilhack, H. et al. (2001) J Cell Biol 152, 325-34.
4. Yi, T. et al. (1993) Mol Cell Biol 13, 7577-86.
5. Wu, C. et al. (2003) Gene 306, 1-12.
6. Bhattacharya, R. et al. (2008) J Mol Signal 3, 8.
7. Zhang, Z. et al. (2003) J Biol Chem 278, 4668-74.
8. Xiao, W. et al. (2010) Blood 116, 6003-13.

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For Research Use Only. Not For Use In Diagnostic Procedures.