Cell Signaling Technology

Product Pathways - Neuroscience

Delta FosB (D3S8R) Rabbit mAb #14695

DeltaFos   DFosB  

No. Size Price
14695S 100 µl ( 10 western blots ) ¥3,100.00 现货查询 购买询价
14695 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 37 Rabbit IgG
IP 1:50

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,

Specificity / Sensitivity

Delta FosB (D3S8R) Rabbit mAb recognizes endogenous levels of total delta FosB protein. This antibody also cross-reacts with an unidentified protein of 85 kDa. This antibody does not cross-react with FosB protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human delta FosB protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 and COS-7 cells, serum-starved overnight and then left untreated (-) or serum-treated (4 hr; +), using Delta FosB (D3S8R) Rabbit mAb (upper), FosB Antibody #2263 (middle), and β-Actin (D6A8) Rabbit mAb #8457 (lower).



Immunoprecipitation of delta FosB from serum-activated NIH/3T3 cell extracts using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or Delta FosB (D3S8R) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using Delta FosB (D3S8R) Rabbit mAb.


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).

The delta FosB protein is encoded by the FosB gene and is produced by alternative splicing. This shorter isoform lacks a carboxy-terminal FosB region that contains ubiquitination sites and results in more stable delta FosB protein (9). Induced delta FosB 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 may represent a molecular switch that helps initiate and maintain the addicted state (14,15).

  1. Tulchinsky, E. (2000) Histol Histopathol 15, 921-8.
  2. Dobrazanski, P. et al. (1991) Mol Cell Biol 11, 5470-8.
  3. Nakabeppu, Y. and Nathans, D. (1991) Cell 64, 751-9.
  4. Rosenberger, S.F. et al. (1999) J Biol Chem 274, 1124-30.
  5. Sasaki, T. et al. (2006) Mol Cell 24, 63-75.
  6. Basbous, J. et al. (2007) Mol Cell Biol 27, 3936-50.
  7. Kovary, K. and Bravo, R. (1991) Mol Cell Biol 11, 2451-9.
  8. Kovary, K. and Bravo, R. (1992) Mol Cell Biol 12, 5015-23.
  9. Carle, T.L. et al. (2007) Eur J Neurosci 25, 3009-19.
  10. Hope, B.T. et al. (1994) Neuron 13, 1235-44.
  11. Nye, H.E. et al. (1995) J Pharmacol Exp Ther 275, 1671-80.
  12. Nye, H.E. and Nestler, E.J. (1996) Mol Pharmacol 49, 636-45.
  13. Chen, J. et al. (1997) J Neurosci 17, 4933-41.
  14. Nestler, E.J. et al. (2001) Proc Natl Acad Sci U S A 98, 11042-6.
  15. McClung, C.A. et al. (2004) Brain Res Mol Brain Res 132, 146-54.

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