Catalog No. | BS64567 |
---|---|
Product Name | RXR alpha (Phospho-S260) polyclonal antibody |
Applications | WB |
Alternative Name | Retinoic acid receptor RXR-alpha; Nuclear receptor subfamily 2 group B member 1; Retinoid X receptor alpha; RXRA; NR2B1 |
Swiss-Prot | P19793 |
Host | Rabbit |
Reactivity | Human,Mouse,Rat |
Application_all | WB: 1:500~1:1000 IHC: 1:50~1:200 |
Product | Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2 |
Purification&Purity | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE). |
Storage&Stability | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. |
Specificity | RXR alpha (Phospho-S260) polyclonal antibody detects endogenous levels of RXR alpha protein only when phosphorylated at Ser260. |
BiowMW | ~ 53 kDa |
Note | For research use only, not for use in diagnostic procedure. |
Immunogen | Synthetic phosphopeptide derived from human RXR alpha around the phosphorylation site of Serine 260. |
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. 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. 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. 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. 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.