RARA, NR1B1, Retinoic acid receptor alpha, Nuclear receptor subfamily 1 group B member 1
Key Feature
Clonality
Monoclonal
Clone Number
EP1823Y
Host Species
Rabbit
Tested Applications
WB
WB:1:500~1000
Species Reactivity
Human
Concentration
1mg/ml
Target Information
Gene Synonyms
NR1B1
Alternative Names
RARA NR1B1 Retinoic acid receptor alpha Nuclear receptor subfamily 1 group B member 1
Molecular Weight(MW)
50771 Da
Function
Receptor 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
Tissue Specificity
A synthetic peptide corresponding to residues near N-terminal of human RAR alpha protein was used as an immunogen.
Cellular Localization
Nucleus. Cytoplasm. Note=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