Cell Signaling Technology

Product Pathways - Neuroscience

Delta FosB Antibody #9890

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M R Mk Endogenous 37 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Delta FosB Antibody recognizes endogenous levels of total Delta FosB and Delta2 Delta FosB proteins. This antibody does not cross-react with FosB.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human Delta FosB protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 cells, serum-starved overnight and then left untreated (-) or treated with serum (4 hrs) (+), using Delta FosB Antibody (upper), or FosB Antibody #2263 (lower).

Western Blotting

Western Blotting

Western blot analysis of extracts from dorsal striatum of mice treated with chronic cocaine (7 days, 20 mg/kg), acute cocaine (6 days saline, 1 day cocaine 20 mg/kg), or saline (7 days), using Delta FosB Antibody (upper). β-Tubulin (9F3) Rabbit mAb #2128 was used as a loading control (lower). Tissue extracts were kindly provided by Dr. Eric Nestler (Mount Sinai School of Medicine, New York).

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), that 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).

Delta FosB is encoded by the FosB gene and is produced by alternative splicing. It lacks the 101 C-terminal residues of FosB, a region containing ubiquitination sites, hence conferring higher stability to Delta FosB (9). Delta FosB is induced and accumulates in select brain regions upon chronic drug use (10-12), where it interacts with JunD to form an active long-lasting AP-1 complex (13). This complex has been proposed to represent a molecular switch that helps initiate and maintain the addicted state (14,15).

  1. Tulchinsky, E. (2000) Histol. Histopathol. 15, 921-928.
  2. Dobrzanski, P. et al. (1991) Mol. Cell. Biol. 11, 5470-5478.
  3. Nakabeppu, Y. and Nathans, D. (1991) Cell 64, 751-759.
  4. Rosenberger, S.F. et al. (1999) J. Biol. Chem. 274, 1124-1130.
  5. Sasaki, T. et al. (2006) Mol. Cell 24, 63-75.
  6. Basbous, J. et al. (2007) Mol. Cell. Biol. 27, 3936-3950.
  7. Kovary, K. and Bravo, R. (1991) Mol. Cell. Biol. 11, 2451-2459.
  8. Kovary, K. and Bravo, R. (1992) Mol. Cell. Biol. 12, 5015-5023.
  9. Carle, T.L. et al. (2007) Eur J Neurosci 25, 3009-3019.
  10. Hope, B.T. et al. (1994) Neuron 13, 1235-1244.
  11. Nye, H.E. et al. (1995) J Pharmacol Exp Ther 275, 1671-1680.
  12. Nye, H.E. and Nestler, E.J. (1996) Mol Pharmacol 49, 636-645.
  13. Chen, J. et al. (1997) J Neurosci 17, 4933-4941.
  14. Nestler, E.J. et al. (2001) Proc Natl Acad Sci USA 98, 11042-11046.
  15. McClung, C.A. et al. (2004) Brain Res Mol Brain Res 132, 146-154.

Application References

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

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