antibody

Anti-Retinoic Acid Receptor, alpha-Isotype

MBS500013

0.1 mL

345 USD

monoclonal

mouse

nonconjugated

763

human, rat

Antibody

Anti-Retinoic Acid Receptor, alpha-Isotype

Retinoic Acid Receptor, a-Isotype

retinoic acid receptor alpha isoform 1; Retinoic acid receptor alpha; retinoic acid receptor alpha; RAR-alpha; retinoic acid receptor, alpha polypeptide; nuclear receptor subfamily 1 group B member 1; retinoic acid nuclear receptor alpha variant 1; retinoic acid nuclear receptor alpha variant 2; nucleophosmin-retinoic acid receptor alpha fusion protein NPM-RAR long form; retinoic acid receptor, alpha; Nuclear receptor subfamily 1 group B member 1

RARA

RARA; RARA; RAR; NR1B1; NR1B1; RAR-alpha

RARA_HUMAN

Monoclonal

IgG1

763

Mouse

Human, rat

462

Immunolabels a ~48kD band in Western Blots of rat brain hippocampal homogenate at antibody dilution of 1:1000.

Protein G purified (Prepared from mouse ascites by ammonium sulfate precipitation followed affinity purification on a Protein G column.)

100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

Store at -20 degree C; stable for at least 1 year.

Western Blot (WB)

Quality Control: Western blots performed on each lot. WB: 1:1000

Antigen: Peptide corresponding to amino acid residues from the N-terminal region of human retinoic acid receptor, alpha-isotype. Immunogen Information: Synthetic peptide corresponding to amino acid residues from the N-terminal region conjugated to KLH. Immunogen Species: Human

Reactivity Assumed Based on 100% Sequence Homology: Bovine, canine, guinea pig and mouse. Species Reactivity Note: The antibody has been directly tested for reactivity in Western blots in rat and human tissues. It is anticipated that the antibody will also work with bovine, canine, mouse and guinea pig tissues based on the fact that these species have 100% homology with the amino acid sequence used as antigen. Biological Significance: Retinoic acid (RA; active metabolite of vitamin A) plays a prominent role in regulating the transition of proliferating precursor cells (such as carcinoma cells and neuronal precursors) to postmitotic differentiated cells (Joshi et al., 2005). The retinoid X receptors (RXRs) family (RXRalpha, beta and gamma), preferentially bind 9-cis-RA and regulate gene transcription by forming heterodimers with a second family of RA receptors. RAs have been suggested to potentially play a therapeutic role in cervical cancer (Abu et al., 2005). RAs are known to play key roles in neuronal development and an increasing body of evidence indicates that retinoid signaling may regulate synaptic plasticity and associated learning and memory behaviors (Lane and Bailey, 2005).

Affinity purified mouse monoclonal antibody.

Abu J, Batuwangala M, Herbert K, Symonds P (2005) Retinoic acid and retinoid receptors: potential chemopreventive and therapeutic role in cervical cancer. Lancet Oncol 6:712-720. Joshi S, Guleria R, Pan J, Dipette D, Singh US (2005) Retinoic acid receptors and tissue-trans-glutaminase mediate short-term effect of retinoic acid on migration and invasion of neuroblastoma SH-SY5Y cells. Oncogene advance online publication 12 September 2005; doi: 10.1038/sj.onc.1209027. Lane MA, Bailey SJ (2005) Role of retinoid signalling in the adult brain. Prog Neurobiol 75:275-293.

4506419

NP_000955.1

NM_000964.3

P10276

48

Acute Myeloid Leukemia Pathway (83117); Acute Myeloid Leukemia Pathway (529); Adipogenesis Pathway (198832); Gene Expression Pathway (105937); Generic Transcription Pathway (105938); IL-3 Signaling Pathway (198881); Integrated Pancreatic Cancer Pathway (711360); Nuclear Receptor Transcription Pathway (105979); Nuclear Receptors Pathway (198848); Nuclear Receptors In Lipid Metabolism And Toxicity Pathway (198887)

This gene represents a nuclear retinoic acid receptor. The encoded protein, retinoic acid receptor alpha, regulates transcription in a ligand-dependent manner. This gene has been implicated in regulation of development, differentiation, apoptosis, granulopoeisis, and transcription of clock genes. Translocations between this locus and several other loci have been associated with acute promyelocytic leukemia. Alternatively spliced transcript variants have been found for this locus.[provided by RefSeq, Sep 2010]

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 KMT2E/MLL5. Mediates retinoic acid-induced granulopoiesis. Ref.19 Ref.22 Ref.23 Ref.24. Subunit structure: Heterodimer; with RXRA. Binds DNA preferentially as a heterodimer. Interacts with CDK7 . By similarity. Interacts with coactivators NCOA3 and NCOA6. Interacts with NCOA7; the interaction requires ligand-binding. Interacts with KMT2E/MLL5. Interacts (via the ligand-binding domain) with PRAME; the interaction is ligand (retinoic acid)-dependent. Interacts with AKT1; the interaction phosphorylates RARA and represses transactivation. Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2. Interacts with PRMT2. Interacts with LRIF1. Interacts with ASXL1 and NCOA1. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.27. Subcellular location: 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. Ref.17 Ref.22. Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. Post-translational modification: 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. Ref.19 Ref.24Sumoylated 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. Ref.17 Ref.22Trimethylation enhances heterodimerization with RXRA and positively modulates the transcriptional activation.Ubiquitinated. Involvement in disease: 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 similarities: Belongs to the nuclear hormone receptor family. NR1 subfamily.Contains 1 nuclear receptor DNA-binding domain. Sequence caution: The sequence AAB00112.1 differs from that shown. Reason: Erroneous initiation. The sequence AAB00113.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB62809.1 differs from that shown. Reason: Erroneous initiation.

0.1 mL

345 USD