Western blot analysis of RAR alpha on different lysates with Rabbit anti-RAR alpha antibody (ER1706-81) at 1/500 dilution.
Lane 1: SK-Br-3 cell lysate
Lane 2: Hela cell lysate
Lysates/proteins at 10 µg/Lane.
Predicted band size: 92 kDa
Observed band size: 92 kDa
Exposure time: 2 minutes;
10% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (ER1706-81) at 1/500 dilution was used in 5% NFDM/TBST at room temperature for 2 hours. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1:300,000 dilution was used for 1 hour at room temperature.
Rabbit polyclonal primary
RAR alpha Rabbit Polyclonal Antibody (ER1706-81)
Recombinant protein within human rar alpha aa 135-406.
SK-Br-3 cell lysate, Hela cell lysate, A431, 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.
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.
Retinoic acid receptor alpha (RAR-α), also known as NR1B1 (nuclear receptor subfamily 1, group B, member 1) is a nuclear receptor that in humans is encoded by the RARA gene. NR1B1 is a gene with a protein product and has a chromosomal location of 17q21.2. RARA codes for the nuclear hormone receptor Retinoic Acid Receptor, Alpha subtype, and are themselves transcription factors. There are another 2 subtypes of RARs, Beta subtype, and Gamma subtype. Retinoid signaling is transduced by 2 families of nuclear receptors, retinoic acid receptor (RAR) and retinoid X receptor (RXR), which form RXR/RAR heterodimers. In the absence of ligand, DNA-bound RXR/RARA represses transcription by recruiting the corepressors NCOR1, SMRT (NCOR2), and histone deacetylase. When ligand binds to the complex, it induces a conformational change allowing the recruitment of coactivators, histone acetyltransferases, and the basic transcription machinery. Retinoic Acid Receptor Alpha, the protein, interacts with retinoic acid, a derivative of Vitamin A, which plays an important role in cell growth, differentiation, and the formation of organs in embryonic development. Once Retinoic Acid binds to the RAR, they initiate transcription and allow for their respective gene to be expressed.
Just like the interactions between antigens and antibodies, the higher the affinity between you and us the better.