Product Pathways - Tyrosine Kinase / Adaptors
Phospho-M-CSF Receptor (Tyr546) Antibody #3083
|W||H M||Transfected Only||175||Rabbit|
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 (Tyr546) Antibody detects transfected levels of M-CSF receptor only when phosphorylated at Tyr546. This antibody may cross-react with other tyrosine-phosphorylated protein tyrosine kinases.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr546 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).
Tyr546 is a major autophosphorylation site in the juxtamembrane domain of the M-CSF receptor. Phosphorylation of Tyr546 plays an important role in the activation of M-CSF (9) and may provide a binding site for downstream signaling components (10).
- 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.
- Schubert, C. et al. (2007) J. Biol. Chem. 282, 4094-4101.
- Joos, H. et al. (1996) J. Biol. Chem. 271, 24476-24481.
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For Research Use Only. Not For Use In Diagnostic Procedures.