Lane 1: Hela
Lane 2: Human lung tissue
Rabbit polyclonal primary
RAR alpha Rabbit Polyclonal Antibody (ER1706-81)
Recombinant protein within human rar alpha aa 135-406.
Hela, human lung tissue lysate, MCF-7, SH-SY5Y, rat brain tissue, mouse testis tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein affinity purified.
NR1B1 antibody; Nuclear mitotic apparatus protein retinoic acid receptor alpha fusion protein antibody; Nuclear receptor subfamily 1 group B member 1 antibody; Nucleophosmin retinoic acid receptor alpha fusion protein NPM RAR long form antibody; RAR alpha antibody; RAR antibody; RAR-alpha antibody; rara antibody; RARA_HUMAN antibody; RARalpha antibody; RARalpha1 antibody; Retinoic acid nuclear receptor alpha variant 1 antibody; Retinoic acid nuclear receptor alpha variant 2 antibody; Retinoic acid receptor alpha antibody; Retinoic acid receptor alpha polypeptide antibody
Belongs to the nuclear hormone receptor family. NR1 subfamily.
Expressed in monocytes.
Phosphorylated 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. Phosphorylated 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 with 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.; Ubiquitinated.; Acetylated; acetylation is increased upon pulsatile shear stress and decreased upon oscillatory shear stress.
Retinoids (RA) are metabolites of vitamin A (retinol) that are important signaling molecules during vertebrate development and tissue differentiation. RAs activate the retinoic acid receptor (RAR) and retinoid X receptor (RXR) nuclear transcription factor families. Most retinoid forms activate RAR family members, whereas RXR family members are activated by 9-cis-RA only. RAR family members, which include RARα, RARβ and RARγ, have a high affinity for all transretinoic acids and belong to the same class of nuclear transcription factors as thyroid hormone receptors, vitamin D3 receptor and ecdysone receptor. RAR isoforms are expressed in distinct patterns throughout development and in the mature organism. The human RARα gene maps to chromosome 17 and is implicated in the chromosomal translocation associated with acute promyelocytic leukemia (APL-M3). Specifically, the RARα gene is fused with the promyelocytic leukemia (PML) gene, which encodes the fusion protein PML/RARα. The PML/RARα fusion protein inhibits PML-dependent apoptotic pathways and halts myeloid differentiation at the promyelocytic stage.