Phospho-CSF-1R/M-CSF-R (Tyr699) (D10B11) Rabbit mAb (BSA and Azide Free) #16975
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 175 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
For standard formulation of this product see product #12251
Storage
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr699 of human CSF-1R/M-CSF-R protein.
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).
Phosphorylation of M-CSF receptor on Tyr669 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery, as well as in another publication (10). Autophosphorylation at Tyr699 in the kinase insert (KI) domain appears to provide a binding site for the Grb2 adaptor protein (9).
- Stanley, E.R. et al. (1978) Nature 274, 168-70.
- Byrne, P.V. et al. (1981) J Cell Biol 91, 848-53.
- Bourette, R.P. and Rohrschneider, L.R. (2000) Growth Factors 17, 155-66.
- Novak, U. et al. (1996) Oncogene 13, 2607-13.
- Bourette, R.P. et al. (1997) EMBO J 16, 5880-93.
- Morley, G.M. et al. (1999) Oncogene 18, 3076-84.
- Toy, E.P. et al. (2001) Gynecol Oncol 80, 194-200.
- Maher, M.G. et al. (1998) Clin Cancer Res 4, 1851-6.
- Hamilton, J.A. (1997) J Leukoc Biol 62, 145-55.
- Downing, J.R. et al. (1991) Mol Cell Biol 11, 2489-95.
Limited Uses
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