Product Pathways - Nuclear Receptor Signaling
RXRβ Antibody #8715
|8715S||100 µl (10 western blots)||---||In Stock||---|
|8715||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Rat, Monkey, Bovine, Dog, Pig.
Specificity / Sensitivity
RXRβ Antibody recognizes endogenous levels of total RXRβ protein. This antibody does not cross-react with either RXRα or RXRγ proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human RXRβ protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from 293T cells, either mock-transfected or transfected with a Myc/DDK-tagged cDNA expression construct encoding full-length human RXRα, RXRβ, and RXRγ, using RXRβ Antibody (upper) or DYKDDDDK Tag Antibody (Binds to same epitope as Sigma's Anti-FLAG® M2 Antibody) #2368 (lower).
The human retinoid X receptors (RXRs) are encoded by three distinct genes (RXRα, RXRβ, and RXRγ) and bind selectively and with high affinity to the vitamin A derivative, 9-cis-retinoic acid. RXRs are type-II nuclear hormone receptors that are largely localized to the nuclear compartment independent of ligand binding. Nuclear RXRs form heterodimers with nuclear hormone receptor subfamily 1 proteins, including thyroid hormone receptor, retinoic acid receptors, vitamin D receptor, peroxisome proliferator-activated receptors, liver X receptors, and farnesoid X receptor (1). Since RXRs heterodimerize with multiple nuclear hormone receptors, they play a central role in transcriptional control of numerous hormonal signaling pathways by binding to cis-acting response elements in the promoter/enhancer region of target genes (2).
RXRβ, like other members of the RXR subfamily, possesses a characteristic tripartite modular structure consisting of (a) a highly conserved central region containing the C4/C5 zinc-finger domain, which is responsible for DNA binding; (b) a relatively well-conserved C-terminal region, which contains the hormone binding and dimerization domains; and (c) a variable N-terminal domain, which has been implicated in either transactivation or repression of target genes (2). Variability within the N-terminal domain is thought to be the result of alternative splicing and/or differential promoter usage (3-5). The murine RXRβ was initially identified because of its ability to bind to the regulatory region II in the murine major histocompatability complex (MHC) class I promoter and is therefore also referred to as H-2RIIBP (6). Genetic ablation of murine Rxrb produced approximately 50% lethality in utero and males that survived had defects of spermatazoa, which resulted in sterility (7). Further studies revealed that expression of a Rxrb mutant with an impaired AF-2 core led to abnormal lipid metabolism in Sertoli cells, suggesting functional interactions between Rxrb and other nuclear receptors that control lipid metabolism (8).
- Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
- Mangelsdorf, D.J. et al. (1992) Genes Dev 6, 329-44.
- Nagata, T. et al. (1994) Gene 142, 183-9.
- Fleischhauer, K. et al. (1993) Hum Genet 90, 505-10.
- Fleischhauer, K. et al. (1992) Nucleic Acids Res 20, 1801.
- Hamada, K. et al. (1989) Proc Natl Acad Sci USA 86, 8289-93.
- Kastner, P. et al. (1996) Genes Dev 10, 80-92.
- Mascrez, B. et al. (2004) EMBO Rep 5, 285-90.
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