Recombinant Human Retinoic acid receptor RXR-alpha (RXRA)

Code CSB-YP020612HU
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Source Yeast
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Code CSB-EP020612HU
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Source E.coli
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Code CSB-EP020612HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP020612HU
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Source Baculovirus
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Code CSB-MP020612HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
RXRA
Uniprot No.
Alternative Names
FLJ00280; FLJ00318; FLJ16020; FLJ16733; MGC102720; NR2B1; Nuclear receptor subfamily 2 group B member 1; OTTHUMP00000022510; Retinoic acid receptor RXR alpha; Retinoic acid receptor RXR-alpha; Retinoid X nuclear receptor alpha; Retinoid X receptor alpha; RXR alpha1; Rxra; RXRA_HUMAN; RXRalpha1
Species
Homo sapiens (Human)
Expression Region
1-462
Target Protein Sequence
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription. The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation. Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA. The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells. Acts as an enhancer of RARA binding to RARE DNA element. May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1. Promotes myelin debris phagocytosis and remyelination by macrophages. Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes. Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence.
Gene References into Functions
  1. the rs11638944:C>G transversion exerts a cis-acting effect on the expression levels of LOXL1, mediated by differential binding of the transcription factor retinoid X receptor alpha and by modulating alternative splicing of LOXL1, eventually leading to reduced levels of LOXL1 mRNA in cells and tissues of risk allele carriers for pseudoexfoliation syndrome PMID: 28534485
  2. RXRA SNPs are not associated with vitamin D status and multiple sclerosis. PMID: 30088172
  3. This review analyzes the non-genomic effects of RXRA in normal and tumor cells, and discusses the functional differences based on RXRA protein structure (structure source: the RCSB Protein Data Bank). [review] PMID: 30093910
  4. The results showed that overexpression of RXRalpha was correlated with unfavorable prognosis, suggesting that RXRalpha may serve as a potential targeted therapeutic marker in the treatment of Esophageal carcinoma (EC). PMID: 29661715
  5. we found that RXRalpha was upregulated in head and neck squamous cell carcinoma PMID: 29228308
  6. Single nucleotide polymorphism rs11185644 near the RXRA was significantly associated with 25-Hydroxyvitamin D dose-response. PMID: 28079136
  7. Variability in the methylation status of the RXRalpha promoter near the EGR transcription factor binding site in newborn cord blood provides controversial epigenetic insights into RXRalpha regulation via EGR proteins. PMID: 29305749
  8. Loss of RXRA is associated with Non-Small Cell Lung Cancer. PMID: 28923935
  9. These findings unveil RXRalpha as an important cellular factor in modulating HBV infection and may point to a new strategy for host-targeted therapies against HBV. PMID: 29437960
  10. RXRalpha regulates HBV replication in and minichromosome remodeling. PMID: 28611266
  11. Findings indicate that Gc globulin (GC) rs16847024, retinoid X receptor gamma (RXRG) rs17429130 and retinoid X receptor alpha (RXRA) rs4917356 were candidate susceptibility markers for gestational diabetes mellitus (GDM) in Chinese females. PMID: 27636996
  12. This suggests that hRXRalpha phosphorylation significantly disrupts its nuclear localization, interaction with VDR, intra-nuclear trafficking, and binding to chromatin of the hVDR-hRXR complex. PMID: 27852823
  13. the expression of CAMP, vitamin D receptor (VDR), and the retinoid X receptor (RXR) isoforms in human skin and gingival tissue biopsies and investigated the signaling pathways involved in 1alpha,25-dihydroxyvitamin D3-induced upregulation of CAMP. PMID: 27357804
  14. IL-1beta upregulated RXRalpha through activation of NF-kappaB signaling. PMID: 26898458
  15. RXRA rs10776909 allele T is specifically involved in the pathogenesis of ChGN. This risk allele may be also associated with worse clinical course of ChGN. PMID: 26610845
  16. Results suggest that retinoid X receptor (RXR) activation protects retinal pigment epithelium (RPE) cells from oxidative stress-induced apoptosis. PMID: 26883505
  17. Data show that pregnane X receptor/retinoid X receptor PXR/RXR-[alpha], RXR-[beta], or RXR-[gamma] expression was noted in 9 (16.4%), 9 (16.4%), and 10 (18.2%) pancreatic adenocarcinoma cases, respectively. PMID: 26355550
  18. Retinoid X receptor alpha plays an important role in proliferation of cholangiocarcinoma PMID: 26310932
  19. Data suggest a potential therapeutic role for the low toxicity synthetic retinoid X receptor selective agonist, UAB30, in neuroblastoma treatment. PMID: 25944918
  20. Studied role of RXRalpha in downregulating hepatic detoxification during inflammation elicited by circulating cytokines. PMID: 26727233
  21. These findings define rules guiding how nuclear receptors integrate two ligand-dependent signalling pathways into RXR heterodimer-specific responses. PMID: 26289479
  22. results reveal the retinoid X receptor pathway as a positive regulator of myelin debris clearance and a key player in the age-related decline in remyelination. PMID: 26463675
  23. DW22 antitumor agent upregulates RXRa and downregulates histone deacetylase in lung cancer and breast cancer tissues and cell lines PMID: 25762635
  24. Vitamin D receptor-retinoid X receptor heterodimer signaling regulates oligodendrocyte progenitor cell differentiation PMID: 26644513
  25. A change in the heterodimeric partner of Peroxisome Proliferator Activated Receptor-alpha from retinoid X receptor to Silent information regulator 1 is responsible for the impaired fatty acid metabolism and cardiac dysfunction in the failing heart. PMID: 26443578
  26. genetic association study in population in France: Data suggest 2 genetic polymorphisms (RXRA, rs7861779; VDR Fok1 [vitamin D receptor Fok1], rs2228570) are associated with cancers related to tobacco use and vitamin D status. PMID: 26447153
  27. interaction of Wnt and RXR-alpha pathways in hepatocyte development and hepatocellular carcinoma PMID: 25738607
  28. SUMOylation of RXRalpha is significantly enhanced through PIAS4-mediated activity. PMID: 26116533
  29. RXRA DNA-binding domain binds to DNA both as a monomer and as a homodimer, and the mechanism of binding is salt dependent and occurs in two steps. PMID: 24824382
  30. the ligand-dependent splicing activity of Acinus is related to the retinoic acid-activated retinoic acid receptor PMID: 25205379
  31. EGCG and IIF cotreatment Cytotoxicity was related to upregulation of 67-kDa laminin receptor (LR67), one of the principal molecular targets of EGCG, and activation of the nuclear retinoic X receptors (RXRs) pathway. PMID: 25013807
  32. These observations suggest that beta-apo-13-carotenone regulates RXRalpha transcriptional activity by inducing the formation of the "transcriptionally silent" RXRalpha tetramer. PMID: 25324544
  33. Data show that disrupting the steroid receptor coactivator-1 (SRC1) binding site on retinoid X receptor alpha (RXRalpha) alters the transactivation by CAR:RXR. PMID: 25053412
  34. elevated methylation at RXRA promoter may be responsible for the downregulated mRNA expression in right ventricular outflow tract myocardium of patients with tetralogy of Fallot PMID: 24513686
  35. Drupanin, a component of BGP, is a novel RXR agonist with slight PPARgamma agonistic activity. PMID: 24972164
  36. The polymorphisms investigated in PPARA (rs1800206), RXRA (rs11381416), and NR1I2 (rs1523130) did not influence the lipid-lowering efficacy and safety of statin and our results show the possible influence of NR1I3 genetic variant on the safety of statin. PMID: 24232815
  37. Retinoid X receptor alpha in human liver is regulated by miR-34a. PMID: 24832862
  38. Low retinoid X receptor alpha expression is associated with colon cancer progression. PMID: 24080207
  39. structural analysis of human retinoid X receptor alpha-liver X receptor beta (RXRalpha-LXRbeta) heterodimer on its cognate element, an AGGTCA direct repeat spaced by 4 nt PMID: 24561505
  40. Data show the networks of interactions that connect retinoid X receptor alpha (RXRalpha) agonists to coactivator GRIP1 binding. PMID: 24187139
  41. MiR-128-2 inhibits the expression of ABCA1, ABCG1 and RXRalpha directly through a miR-128-2-binding site within their respective 3'untranslated regions. PMID: 23990020
  42. Inflammatory signaling pathways rapidly induce SUMOylation of RXRalpha. PMID: 23690070
  43. SNPs in the CYP24A1, CYP2R1, calcium sensing receptor (CASR), vitamin D binding protein (GC), retinoid X receptor-alpha (RXRA) and megalin (LRP2) genes were significantly associated with pancreas cancer risk. PMID: 23826131
  44. These structures establish that PXR and RXRalpha form a heterotetramer unprecedented in the nuclear receptor family of ligand-regulated transcription factors. PMID: 23602807
  45. Retinoid acid receptor expression is helpful to distinguish between adenoma and well-differentiated carcinoma in the thyroid. PMID: 23639973
  46. data demonstrate that GSK-3beta plays an important role in regulating tRXRalpha production by calpain II in cancer cells PMID: 23389291
  47. RXRalpha diminishes cytoprotection by NRF2 by binding directly to the newly defined Neh7 domain in NRF2. PMID: 23612120
  48. Polymorphisms in the RXRA and NR1I3 genes influence lipid profile in a Southern Brazilian population. PMID: 23079705
  49. Expression of TauT is differentially regulated by Vitamin D(3) and retinoic acid via formation of VDR and RXR complexes in the nuclei in a cell type-dependent manner. PMID: 23392891
  50. Single nucleotide polymorphisms in the RXRA and PLAUR genes in the vitamin D pathway may contribute to breast cancer disease free survival. PMID: 23180655

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Subcellular Location
Nucleus. Cytoplasm. Mitochondrion.
Protein Families
Nuclear hormone receptor family, NR2 subfamily
Tissue Specificity
Expressed in lung fibroblasts (at protein level). Expressed in monocytes. Highly expressed in liver, also found in kidney and brain.
Database Links

HGNC: 10477

OMIM: 180245

KEGG: hsa:6256

STRING: 9606.ENSP00000419692

UniGene: Hs.590886

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