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Validated All-in-One™ qPCR Primer for RXRA(NM_002957.5) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcriptional regulators. [provided by RefSeq].
Gene References into function
- The role of retinoid X receptor messenger RNA expression in curatively resected non-small cell lung cancer
- Retinoid signaling is attenuated by retinoic acid-induced proteasome-mediated degradation of RXRA in human keratocytes.
- the effect of STAT5b-RARalpha on the activity of myeloid transcription factors including RARalpha/retinoid X receptor (RXR) alpha
- Interactions that determine the assembly of a retinoid X receptor/corepressor complex
- retinoid x receptor alpha structural results support the idea that docosa hexaenoic acid and related fatty acids could be natural agonists of RXRs
- RXR alpha responsive element-dependent expression and RXR alpha-dependent transcriptional activation is regulated in T lymphocytes by cellular Ser/Thr phosphatases PP1 and PP2A.
- regulates vitamin D receptor functions in part by regulating subcellular localization
- Results demonstrate that human papilloma virus 16 E6 oncoprotein inhibits the RXR(alpha)-mediated transactivation of target genes, implying that perturbation of RXR-mediated transactivation by E6 could contribute to HPV oncogenesis.
- in response to retinoic acid and in a manner requiring the activity of RXRalpha, secretes trophic factors which drive fetal cardiomyocyte proliferation and promote ventricular chamber morphogenesis
- IL-3-induced enhancement of retinoic acid receptor activity is mediated through Stat5, which physically associates with recombinant human retinoic acid receptors in an IL-3-dependent manner.
- With PPAR-gamma, forms heterodimers in the regulation of human trophoblast invasion
- RXRalpha and RXRgamma immunodetected in all normal, nodular, and basal cell hyperplasia, as well as carcinomatous prostates. In atrophic glands, the expression of both receptors was found in 22.5% of samples.
- results suggest that oxidized phospholipids inhibit transcription of the thrombomodulin gene in vascular endothelium by inhibiting the binding of retinoic acid receptor beta-retinoid x receptor alpha heterodimer and Sp1 and Sp3 to thrombomodulin promoter
- RXR and its agonists have roles in the regulation of beta-catenin turnover and related biological events
- Transcriptionlal activation driven by the PPARalpha/RXRalpha complex was counteracted by the expression of ERRalpha in HeLa cells.
- RXRalpha up-regulation was associated with the early stages of laryngeal carcinogenesis
- Expression of adipophilin is enhanced during trophoblast differentiation and is up-regulated by ligand-activated PPARgamma/retinoid X receptor. May contribute to fatty acid uptake by placenta.
- depletion of vitamin A and retinoid receptors by UV irradiation, together with unchanged or even increased c-Jun levels, might seriously interfere with retinoid signaling and thus promote future tumor development, especially in keratinocytes.
- Retinoid x receptor alpha (RXRalpha) may be actively involved in cell proliferation and cell cycle regulation in human hepatocyte cell line Hep3B cells.
- results suggest a novel function of RNF8 as a regulator of RXR alpha-mediated transcriptional activity through interaction between their respective N-terminal regions
- Decrease of RXRalpha in prostate basal cells may serve as a marker for prostate carcinoma-associated field change, which may represent an early event in the prostate carcinogenic process.
- RXR could function as a fatty acid receptor in vivo.
- Data suggest that altered localization of retinoid X receptor alpha to the splicing factor compartment may be an important factor for the loss of retinoid responsiveness in MDA-MB-231 breast cancer cells.
- Casein kinase 1alpha interacts with retinoid X receptor and interferes with agonist-induced apoptosis
- Results show an increased DNA binding of the retinoic acid receptor alpha/retinoid X receptor alpha heterodimer and the stability of nuclear localization of this heterodimer, which facilitates signal transduction.
- Increase in expression of RXRalpha is associated with esophageal squamous cell carcinomas
- study indicated that the subcellular intratumoral distribution pattern of RXR-alpha could independently predict the survival of RCC patients
- novel aspect of RXRalpha function: it acts as a carrier for nucleocytoplasmic translocation of orphan receptors
- nongenotropic function of RXRalpha and its involvement in the regulation of the Nur77-dependent apoptotic pathway
- results suggest specific physiological roles of two novel human RXR alpha splice variants
- The receptor, alpha shows abundant expression in the variety of tissues.
- The results obtained using truncated PGC-1alpha proteins suggested that two regions are necessary for PGC-1alpha to interact with the DNA-binding complex of RXRalpha/FXR.
- These results indicate that the RXRalpha gene is transcribed at stable levels, similar to most housekeeping genes, and its transcription is regulated by ATRA.
- Results suggest that the binding of PPARbeta-specific ligand enhances the affinity between RXRalpha and activated PPARbeta and thus may regulate angptl3 gene expression through a DR4 element by competing with LXRalpha for RXRalpha.
- SUSP1 plays an important role in the control of the transcriptional activity of RXRalpha and thus in the RXRalpha-mediated cellular processes
- metabolism of a parent compound, beta-carotene, may alternatively activate (9-cisRA) or inhibit (beta-apo-14'-carotenal) specific RXR and PPAR responses
- Down-regulation of RXRalpha is critically required for neutrophil development since ectopic RXRalpha inhibited granulopoiesis by impairing proliferation and differentiation
- in addition to the induction of coactivator peptide binding, all well-known RXRalpha agonists also induce binding of corepressor peptides to RXRalpha
- Accumulation of full-length retinoid X receptor alpha (RXRalpha) in leiomyomas that is not associated with a modification of its gene expression.
- our results indicate that activator Sp1 and repressor RXRalpha:RARalpha act in concert to regulate MRP3 expression.
- A marginally significant increase in AA allelic frequency of the RXRA A39526AA polymorphism in plaque psoriatic men compared to healthy men was proved.
- VDR and retinoid X receptor alpha (RXRalpha) binds to the VDRE and increases PLD1 gene expression in HaCaT cells.
- RARalpha/RXRalpha heterodimer is involved in the differential regulation of the GnRH II gene in neuronal and placental cells.
- Inhibition of RXRalpha phosphorylation and restoration of its original function as a regulator of nuclear receptors might be an effective strategy for controlling cancer cell growth.
- analysis of the interaction differences of two synthetic modulators of RXRalpha LBD
- phosphorylation of RXRalpha at serine 260 impaired the recruitment of DRIP205 and other coactivators to the VDR.RXRalpha complex
- in PC-3 cells, RXR-alpha is not required for the nuclear translocation of IGFBP-3 and that IGFBP-3 can induce apoptosis in human prostate cancer cells without binding RXR-alpha.
- RXR ligands rapidly inhibit high-glucose-induced oxidative stress by antagonizing high-glucose-induced PKC activation, and cytoplasmic RXRalpha is implicated in this regulation
- PPARgamma/retinoid X receptor complex released from activated platelets in microparticles was internalized by a monocytic cell line.
- The nuclear hormone receptors hepatocyte nuclear factor 4 (HNF4) and retinoid X receptor alpha (RXRalpha) support hepatitis B virus (HBV) pregenomic RNA synthesis and viral replication in nonhepatoma cells.
- Activation of the thyroid hormone receptor beta/retinoid X receptor alpha heterodimer by T(3) stimulated expression of the hepatic leukemia factor, which increases HIF-1alpha gene expression.
- Vitamin D receptor (VDR) with the retinoid X receptor (RXR) recruits NCoR and SMRT strictly in a VDR agonist-dependent manner.
- Fluorophore-labelled RXRalpha ligand- binding domain (LBD) can be viewed as a molecular sensor that is predictive of the crystallization potential of RXRalpha LBD complexes; this system could be applicable to other nuclear receptor LBDs.
- A functional role of PPARgamma/RXRalpha and Oct-1 in the regulation of the FABP2 gene.
- A/B and C domains of RXR and the ability of RXR to form homodimers are required for rexinoid-driven growth inhibition, caspase activation and subsequent apoptosis.
- 9-cis RA regulation of RXRalpha mitochondrial translocation depends on mitochondrial membrane potential and ATP.
- bexarotene increased the occupancy of the identified enhancer element in IGFBP-6 gene by RXRalpha, RARbeta, cJun, cFos, and p300
- structures of intact PPAR-gamma and RXR-alpha as a heterodimer bound to DNA, ligands and coactivator peptides
- Term human labour is associated with changes in expression and activity of PPAR isoforms and its transcription partner, RXRalpha.
