Product Pathways - Neuroscience
Delta FosB Antibody #9890
|9890S||100 µl (10 western blots)||---||In Stock||---|
|9890||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||37||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
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 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 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).
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).
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