Product Pathways - Phosphatases
SHP-1 (C14H6) Rabbit mAb #3759
| Applications | Reactivity | MW (kDa) | Source | Isotype |
|---|---|---|---|---|
| W IP | H M (R) | 68 | Rabbit | IgG |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
SHP-1 (C14H6) Rabbit mAb detects endogenous level of total SHP-1 protein.
Source / Purification
Monoclonal antibody is produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Pro161 of human SHP-1.
Background
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 down regulate several tyrosine kinase regulated pathways. In hematopoietic cells, the N-terminal SH2 domain of SHP-1 binds to tyrosine phosphorylated erythropoietin receptors (EpoR) to negatively regulate hematopoietic growth (2). Over expression 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 IL-3R β chain and down regulates IL-3-induced tyrosine phosphorylation and cell proliferation (4). Because SHP-1 down regulates various proliferation pathways, SHP-1 is considered a potential tumor suppressor and angiogenesis regulator (5,6).
- Yi, T.L. et al. (1992) Mol Cell Biol 12, 836-46.
- Yi, T. et al. (1995) Blood 85, 87-95.
- Keilhack, H. et al. (2001) J Cell Biol 152, 325-34.
- Yi, T. et al. (1993) Mol Cell Biol 13, 7577-86.
- Wu, C. et al. (2003) Gene 306, 1-12.
- Bhattacharya, R. et al. (2008) J Mol Signal 3, 8.
Application References
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