Product Pathways - Nuclear Receptor Signaling
RXRα Antibody #5388
|W IP||H R Mk||Endogenous||53||Rabbit|
Reactivity Key: H=Human 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.
Specificity / Sensitivity
RXRα Antibody recognizes endogenous levels of total RXRα protein. RXRα Antibody does not cross-react with either RXRβ or RXRγ.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human RXRα protein. Antibodies are purified by protein A and peptide affinity chromatography.
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).
Retinoid X receptor α (RXRα) is the founding RXR family member and is predominantly expressed in liver, kidney, epidermis, intestine and a variety of tissues (2-4). Knockout of the murine rxrα gene results in embryonic lethality tentatively due to myocardial hypoplasia, which demonstrates the importance of RXRα to retinoid signaling in vivo (5,6). Biochemical evidence suggests that RXRα transcriptional activity is post-translationally regulated through the Ras-Raf-MAPK signaling cascade. MAPK-dependent phosphorylation of RXRα directly abrogates the ability of RXRα to associate with nuclear receptor coactivators (7).
- Gronemeyer, H. et al. (2004) Nat Rev Drug Discov 3, 950-64.
- Mangelsdorf, D.J. et al. (1992) Genes Dev 6, 329-44.
- Mangelsdorf, D.J. et al. (1990) Nature 345, 224-9.
- Dollé, P. et al. (1994) Mech Dev 45, 91-104.
- Kastner, P. et al. (1994) Cell 78, 987-1003.
- Sucov, H.M. et al. (1994) Genes Dev 8, 1007-18.
- Macoritto, M. et al. (2008) J Biol Chem 283, 4943-56.
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For Research Use Only. Not For Use In Diagnostic Procedures.