Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-M-CSF Receptor (Tyr723) Antibody #3151

Applications Reactivity Sensitivity MW (kDa) Source
W H M Endogenous 175 Rabbit

Applications Key:  W=Western Blotting
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.

Protocols

Specificity / Sensitivity

Phospho-M-CSF Receptor (Tyr723) Antibody detects endogenous M-CSF receptor only when phosphorylated at tyrosine 723.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr723 of human M-CSF receptor. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from GDM-1 cells, untreated or λ phosphatase-treated, using Phospho-M-CSF Receptor (Tyr723) Antibody (upper) or M-CSF Receptor Antibody #3152 (lower).

Background

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).

  1. Stanley, E. R. et al. (1978) Nature 274, 168-170.
  2. Byrne, P. V. et al. (1981) J. Cell. Biol. 91, 848-853.
  3. Bourette, R. P. et al. (2000) Growth Factors 17, 155-166.
  4. Novak, U. et al. (1996) Oncogene 13, 2607-2613.
  5. Bourette, R. P. et al. (1997) EMBO J. 16, 5880-5893.
  6. Morley, G. M. et al. (1999) Oncogene 18, 3076-3084.
  7. Toy, E. P. et al. (2001) Gynecol. Oncol. 80, 194-200.
  8. Maher, M. G. et al. (1998) Clin. Cancer Res. 4, 1851-1856.

Application References

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

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