Product nameAnti-Retinoid X Receptor alpha/RXRA antibody
See all Retinoid X Receptor alpha/RXRA primary antibodies
DescriptionRabbit polyclonal to Retinoid X Receptor alpha/RXRA
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Mouse, Human
Synthetic peptide corresponding to Human Retinoid X Receptor alpha/RXRA conjugated to keyhole limpet haemocyanin.
- An induced culture of E. coli
This product was previously labelled as Retinoid X Receptor alpha
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Storage bufferPreservative: 0.01% Thimerosal (merthiolate)
Concentration information loading...
PurityImmunogen affinity purified
- Signal Transduction
- Signaling Pathway
- Nuclear Signaling
- Nuclear Hormone Receptors
- Retinoic & Retinoid
- Pathways and Processes
- Metabolic signaling pathways
- Lipid and lipoprotein metabolism
- Lipid metabolism
Our Abpromise guarantee covers the use of ab86027 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
FunctionReceptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and 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. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes.
Tissue specificityHighly expressed in liver, also found in lung, kidney and heart.
Sequence similaritiesBelongs to the nuclear hormone receptor family. NR2 subfamily.
Contains 1 nuclear receptor DNA-binding domain.
DomainComposed of three domains: a modulating N-terminal domain (AF1 domain), a DNA-binding domain and a C-terminal ligand-binding domain (AF2 domain).
modificationsPhosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Constiutively phosphorylated on Ser-21 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity). Phosphorylated on Ser-27, in vitro, by PKA. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA.
Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6.
- Information by UniProt
- FLJ00280 antibody
- FLJ00318 antibody
- FLJ16020 antibody
All lanes : Anti-Retinoid X Receptor alpha/RXRA antibody (ab86027) at 1/1000 dilution
Lane 1 : An un-induced culture of E. coli
Lane 2 : An induced culture of E. coli
Lysates/proteins at 1/5000 dilution per lane.
All lanes : Anti-Rabbit IgG HRP at 1/1000 dilution
Predicted band size: 51 kDa
Observed band size: 65 kDa why is the actual band size different from the predicted?
Additional bands at: 45 kDa, 46 kDa. We are unsure as to the identity of these extra bands.
Exposure time: 60 minutes
Gel concentration 10%Predicted molecular weight of Retinoid X Receptor alpha/RXRA 64.8kDa (50.8kDa + another 14kDa for the tag).
ab86027 has not yet been referenced specifically in any publications.