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Use Anti-Estrogen Receptor β Antibody, clone 9.88 (Mouse Monoclonal Antibody) validated in WB, IP to detect Estrogen Receptor β also known as Estrogen receptor beta.
More>>Use Anti-Estrogen Receptor β Antibody, clone 9.88 (Mouse Monoclonal Antibody) validated in WB, IP to detect Estrogen Receptor β also known as Estrogen receptor beta. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Estrogen receptor beta (ERβ; NR3A2 or ESR2) is a nuclear steroid receptor that has been detected in the ovary, testis, thymus, spleen, bone, brain, and kidney. It is a multidomain protein containing A/B, C, D, E, and F domains, and it is activated by estrogen, resulting in homo- or heterodimerization (with ERα). The active ERβ-estrogen complex binds to regulatory regions known as estrogen response elements on target genes; however, ERβ may also regulate transcription without a bound ligand via its activation function (AF-1) region in the A/B domain. The ERβ receptor interacts with a wide variety of proteins including transcriptional corepressors and coactivators that regulate its activity. Its expression is also regulated by hypermethylation of CpG islands in the ERβ promoter. Previous studies have reported that ERβ has anti-inflammatory and anti-proliferative effects, and may therefore be an important therapeutic target for cancers, especially those occurring in the reproductive organs.
References
Product Information
Format
Purified
Control
PC-12 cell lysate
Presentation
Purified mouse monoclonal IgMκ in buffer containing PBS with 0.05% sodium azide.
Use Anti-Estrogen Receptor β Antibody, clone 9.88 (Mouse Monoclonal Antibody) validated in WB, IP to detect Estrogen Receptor β also known as Estrogen receptor beta.
Key Applications
Western Blotting
Immunoprecipitation
Application Notes
Immunoprecipitation Analysis: A representative lot from an independent laboratory immunoprecipitated Estrogen Receptor β in HUVEC cells (Simoncini, T., et al. (2006). Mol Endocrinol. 20(8):1756-1771.).
Biological Information
Immunogen
Recombinant protein corresponding to human Estrogen Receptor β.
This gene encodes a member of the family of estrogen receptors and superfamily of nuclear receptor transcription factors. The gene product contains an N-terminal DNA binding domain and C-terminal ligand binding domain and is localized to the nucleus, cytoplasm, and mitochondria. Upon binding to 17beta-estradiol or related ligands, the encoded protein forms homo- or hetero-dimers that interact with specific DNA sequences to activate transcription. Some isoforms dominantly inhibit the activity of other estrogen receptor family members. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been fully characterized.
FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual.
SUBUNIT STRUCTURE: Binds DNA as a homodimer. Can form a heterodimer with ESR1. Interacts with NCOA3, NCOA5 and NCOA6 coactivators, leading to a strong increase of transcription of target genes. Interacts with PELP1 and UBE1C. Isoform beta-2/cx preferentially forms a hetereodimer with ESR1 rather than ESR2 and inhibits DNA-binding by ESR1. Interacts with AKAP13. Interacts with DNTTIP2. Interacts with isoform 4 of TXNRD1. Interacts with CCDC62 in the presence of estradiol/E2; this interaction seems to enhance the transcription of target genes, including cyclin-D1/CCND1 AP-1 promoter. Interacts with DYX1C1. Interacts with PRMT2. Interacts with PRMT2.
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Isoform beta-1 is expressed in testis and ovary, and at a lower level in heart, brain, placenta, liver, skeletal muscle, spleen, thymus, prostate, colon, bone marrow, mammary gland and uterus. Also found in uterine bone, breast, and ovarian tumor cell lines, but not in colon and liver tumors. Isoform beta-2 is expressed in spleen, thymus, testis and ovary and at a lower level in skeletal muscle, prostate, colon, small intestine, leukocytes, bone marrow, mammary gland and uterus. Isoform beta-3 is found in testis. Isoform beta-4 is expressed in testis, and at a lower level in spleen, thymus, ovary, mammary gland and uterus. Isoform beta-5 is expressed in testis, placenta, skeletal muscle, spleen and leukocytes, and at a lower level in heart, lung, liver, kidney, pancreas, thymus, prostate, colon, small intestine, bone marrow, mammary gland and uterus. Not expressed in brain.
DOMAIN: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
SEQUENCE SIMILARITIES: Belongs to the nuclear hormone receptor family. NR3 subfamily. Contains 1 nuclear receptor DNA-binding domain.
SEQUENCE CAUTION: The sequence CAA67555.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
Molecular Weight
~55 kDa observed. Uniprot describes eight different isoforms ranging from ~36 kDa to ~59 kDa.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in PC-12 cell lysate.
Western Blot Analysis: A 1:1,000 dilution of this antibody detected Estrogen Receptor β in PC-12 cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Estrogen receptor alpha interacts with Galpha13 to drive actin remodeling and endothelial cell migration via the RhoA/Rho kinase/moesin pathway. Simoncini, Tommaso, et al. Mol. Endocrinol., 20: 1756-71 (2006)
2005
Sex steroids control cell movement and tissue organization; however, little is known of the involved mechanisms. This report describes the ongoing dynamic regulation by estrogen of the actin cytoskeleton and cell movement in human vascular endothelial cells that depends on rapid activation of the actin-regulatory protein moesin. Moesin activation is triggered by the interaction of the C-terminal portion of cell membrane estrogen receptor alpha with the G protein Galpha(13), leading to activation of the small GTPase RhoA and of the downstream effector Rho-associated kinase. The resulting phosphorylation of moesin on Thr(558) is the means of moesin's binding to actin and the remodeling of the actin cytoskeleton. This cascade of events ensues within minutes of estradiol administration and results in changes in cell morphology and to the development of specialized cell membrane structures such as ruffles and pseudopodia that are necessary for cell movement. These findings expand our knowledge of the basis of estrogen's effects on human cells, including the regulation of actin assembly, cell movement and migration. They highlight novel pathways of signal transduction of estrogen receptor alpha through nontranscriptional mechanisms. Furthermore, exposure of this estrogen receptor-dependent, nongenomic action of estrogen on human vascular endothelial cells is especially relevant to the present interest in the role of estrogen in cardiovascular protection.
