Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

RXRβ Antibody #8715

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M (R) (Mk) (B) (Dg) (Pg) Endogenous 70-72 Rabbit

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

Protocols

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 Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using RXRβ Antibody.

Isoform Specificity

Isoform Specificity

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).

Background

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).

  1. Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
  2. Mangelsdorf, D.J. et al. (1992) Genes Dev 6, 329-44.
  3. Nagata, T. et al. (1994) Gene 142, 183-9.
  4. Fleischhauer, K. et al. (1993) Hum Genet 90, 505-10.
  5. Fleischhauer, K. et al. (1992) Nucleic Acids Res 20, 1801.
  6. Hamada, K. et al. (1989) Proc Natl Acad Sci USA 86, 8289-93.
  7. Kastner, P. et al. (1996) Genes Dev 10, 80-92.
  8. Mascrez, B. et al. (2004) EMBO Rep 5, 285-90.

Application References

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

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