Phospho-c-Fos (Ser32) (D82C12) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) #8709
- F
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-c-Fos (Ser32) (D82C12) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate) detects endogenous levels of c-Fos protein only when phosphorylated at Ser32. The antibody does not cross-react with other Fos proteins, including FosB, FRA1, and FRA2.
Species Reactivity:
Human, Mouse, Rat
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Hamster, Monkey, Bovine, Pig, Horse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to Ser32 of human c-Fos protein.
Background
The Fos family of nuclear oncogenes includes c-Fos, FosB, Fos-related antigen 1 (FRA1), and Fos-related antigen 2 (FRA2) (1). While most Fos proteins exist as a single isoform, the FosB protein exists as two isoforms: full-length FosB and a shorter form, FosB2 (Delta FosB), which lacks the carboxy-terminal 101 amino acids (1-3). The expression of Fos proteins is rapidly and transiently induced by a variety of extracellular stimuli, including growth factors, cytokines, neurotransmitters, polypeptide hormones, and stress. Fos proteins dimerize with Jun proteins (c-Jun, JunB, and JunD) to form Activator Protein-1 (AP-1), a transcription factor that binds to TRE/AP-1 elements and activates transcription. Fos and Jun proteins contain the leucine-zipper motif that mediates dimerization and an adjacent basic domain that binds to DNA. The various Fos/Jun heterodimers differ in their ability to transactivate AP-1 dependent genes. In addition to increased expression, phosphorylation of Fos proteins by Erk kinases in response to extracellular stimuli may further increase transcriptional activity (4-6). Phosphorylation of c-Fos at Ser32 and Thr232 by Erk5 increases protein stability and nuclear localization (5). Phosphorylation of FRA1 at Ser252 and Ser265 by Erk1/2 increases protein stability and leads to overexpression of FRA1 in cancer cells (6). Following growth factor stimulation, expression of FosB and c-Fos in quiescent fibroblasts is immediate, but very short-lived, with protein levels dissipating after several hours (7). FRA1 and FRA2 expression persists longer, and appreciable levels can be detected in asynchronously growing cells (8). Deregulated expression of c-Fos, FosB, or FRA2 can result in neoplastic cellular transformation; however, Delta FosB lacks the ability to transform cells (2,3).
- Tulchinsky, E. (2000) Histol Histopathol 15, 921-8.
- Dobrazanski, P. et al. (1991) Mol Cell Biol 11, 5470-8.
- Nakabeppu, Y. and Nathans, D. (1991) Cell 64, 751-9.
- Rosenberger, S.F. et al. (1999) J Biol Chem 274, 1124-30.
- Sasaki, T. et al. (2006) Mol Cell 24, 63-75.
- Basbous, J. et al. (2007) Mol Cell Biol 27, 3936-50.
- Kovary, K. and Bravo, R. (1991) Mol Cell Biol 11, 2451-9.
- Kovary, K. and Bravo, R. (1992) Mol Cell Biol 12, 5015-23.
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