RXRα Antibody #5388
- WB
- IP
Supporting Data
| REACTIVITY | H R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 53 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Protocol
Specificity / Sensitivity
RXRα Antibody recognizes endogenous levels of total RXRα protein. RXRα Antibody does not cross-react with either RXRβ or RXRγ.
Species Reactivity:
Human, Rat, Monkey
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.
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).
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).
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