Anti-Retinoic Acid Receptor alpha antibody (ab66777)
- Product nameAnti-Retinoic Acid Receptor alpha antibodySee all Retinoic Acid Receptor alpha primary antibodies ...
- DescriptionRabbit polyclonal to Retinoic Acid Receptor alpha
- Tested applicationsWB more details
- Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthetic peptide: MYESVEVGGP TPNPFLVVDF YNQNRACLLP EKGLPAPGPY STPLRTPLWN, corresponding to a region within N terminal amino acids 1-50 of Human Retinoic Acid Receptor alpha
- Positive controlJurkat cell lysate.
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: None
Constituents: 2% Sucrose, PBS
- Concentration information loading...
- PurityProtein A purified
- Clonality Polyclonal
- Signal Transduction
- Signaling Pathway
- Nuclear Signaling
- Nuclear Hormone Receptors
- Retinoic & Retinoid
Our Abpromise guarantee covers the use of ab66777 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||WB: Use a concentration of 1.25 µg/ml. Detects a band of approximately 45 kDa (predicted molecular weight: 51 kDa). Good results were obtained when blocked with 5% non-fat dry milk in 0.05% PBS-T.|
- 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 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. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Regulates expression of target genes in a ligand-dependent manner by recruiting chromatin complexes containing MLL5. Mediates retinoic acid-induced granulopoiesis.
- Involvement in diseaseNote=Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation.
- Sequence similaritiesBelongs to the nuclear hormone receptor family. NR1 subfamily.
Contains 1 nuclear receptor DNA-binding domain.
- DomainComposed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
modificationsPhosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for transcriptional activity (By similarity). Phosphorylation by AKT1 is required for the repressor activity but has no effect on DNA binding, protein stability nor subcellular localization. Phosporylated by PKA in vitro. This phosphorylation on Ser-219 and Ser-369 is critical for ligand binding, nuclear localization and transcriptional activity in response to FSH signaling.
Sumoylated by SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity.
Trimethylation enhances heterodimerization with RXRA and positively modulates the transcriptional activation.
- Cellular localizationNucleus. Cytoplasm. Nuclear localization depends on ligand binding, phosphorylation and sumoylation. Transloaction to the nucleus in the absence of ligand is dependent on activation of PKC and the downstream MAPK phosphorylation.
- Acute Promelocytic Leukemia Breakpoint Cluster Region antibodyNR1B1 antibodyNuclear mitotic apparatus protein retinoic acid receptor alpha fusion protein antibody
- Nuclear receptor subfamily 1 group B member 1 antibodyNucleophosmin retinoic acid receptor alpha fusion protein NPM RAR long form antibodyRAR A antibodyRAR alpha antibodyRAR alpha form antibodyRAR antibodyRAR-alpha antibodyRARA antibodyRARA protein antibodyRARA/PML Fusion Gene antibodyRARA_HUMAN antibodyRARalpha antibodyRARalpha1 antibodyRetinoic acid receptor alpha antibodyRetinoic acid receptor alpha polypeptide antibody
Anti-Retinoic Acid Receptor alpha antibody images
All lanes : Anti-Retinoic Acid Receptor alpha antibody (ab66777) at 1.25 µg/ml (in 5% skim milk / PBS buffer)
Lane 1 : Molecular weight markers
Lane 2 : Jurkat cell lysate at 10 µg
HRP conjugated anti-Rabbit IgG at 1/50000 dilution
Predicted band size : 51 kDa
Observed band size : 45 kDa (why is the actual band size different from the predicted?)
Additional bands at : 64 kDa. We are unsure as to the identity of these extra bands.
References for Anti-Retinoic Acid Receptor alpha antibody (ab66777)
ab66777 has not yet been referenced specifically in any publications.