Product Pathways - Tyrosine Kinase / Adaptors
Phospho-M-CSF Receptor (Tyr923) Antibody #3406
Reactivity Key: H=Human M=Mouse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-M-CSF Receptor (Tyr923) Antibody detects endogenous levels of M-CSF receptor only when phosphorylated at Tyr923. The antibody may cross-react with other activated tyrosine kinases including PDGF and FGF receptors.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues around Tyr923 of human M-CSF receptor. Antibodies are purified by protein A and peptide affinity chromatography.
Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).
The equivalent site (Tyr921) of Tyr923 in human M-CSF receptor was demonstrated to be phosphorylated in mouse macrophages in a CSF-1 stimulation dependent manner (10). Phosphorylation of Tyr923 of M-CSF receptor may provide a docking site for Grb2 binding (9).
- Stanley, E. R. et al. (1978) Nature 274, 168-170.
- Byrne, P. V. et al. (1981) J. Cell. Biol. 91, 848-853.
- Bourette, R. P. et al. (2000) Growth Factors 17, 155-166.
- Novak, U. et al. (1996) Oncogene 13, 2607-2613.
- Bourette, R. P. et al. (1997) EMBO J. 16, 5880-5893.
- Morley, G. M. et al. (1999) Oncogene 18, 3076-3084.
- Toy, E. P. et al. (2001) Gynecol. Oncol. 80, 194-200.
- Maher, M. G. et al. (1998) Clin. Cancer Res. 4, 1851-1856.
- Mancini, A. et al. (1997) Oncogene 15, 1565-72.
- Yu, W. et al. (2008) J Leukoc Biol 84, 852-63.
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For Research Use Only. Not For Use In Diagnostic Procedures.