CSF-1R/M-CSF-R Antibody #3152
- WB
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 52 cytoplasmic domain. 140 precursor. 175 M-CSF Receptor. |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
After initial dimerization and autophosphorylation, the CSF-1 receptor undergoes regulated intramembrane proteolysis (RIP) that involves proteolytic processing of this membrane protein and results in release of extracellular domain, intramembrane cleavage and release of the cytoplasmic domain into the cytosol (9). The activated intracellular domain then moves to the nucleus and regulates transcription of specific genes (10). It has been shown that the processing and down modulation of CSF-1 receptor is a continuous process and its rate increases substantially in response to a variety of stimuli including PMA, LPS, tumor necrosis factor, IL-2, Il-4 and its physiological ligand CSF-1 (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.
- Wilhelmsen, K. and van der Geer, P. (2004) Mol Cell Biol 24, 454-64.
- Urban, S. and Freeman, M. (2002) Curr Opin Genet Dev 12, 512-8.
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