|Product Name||Anti-Estrogen Receptor beta/ESR2 Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Estrogen receptor beta(ESR2) detection. Tested with WB in Human.|
|Cite This Product||Anti-Estrogen Receptor beta/ESR2 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1126)|
|Immunogen||A synthetic peptide corresponding to a sequence at the N-terminus of human Estrogen Receptor beta(27-50aa HGSIYIPSSYVDSHHEYPAMTFYS), different from the related rat and mouse sequences by four amino acids.|
Assay Dilutions Overview
Western blot, 0.1-0.5μg/ml, Human
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
Images And Assay Conditions
Anti-Estrogen Receptor beta antibody, PA1126, Western blotting
WB: MCF-7 Cell Lysate
Protein Target Info (Source: Uniprot.org)
|Protein Name||Estrogen receptor beta|
|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.|
|Alternative Names||Estrogen receptor beta;ER-beta;Nuclear receptor subfamily 3 group A member 2;ESR2;ESTRB, NR3A2;|
|Subcellular Localization||Nucleus .|
|Molecular Weight||59216 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein 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 (PubMed:20074560). 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. .|
|Research Areas||Cancer, Chip'Ing Antibodies, Diabetes, Domain Families, Endocrine System, Epigenetics And Nuclear Signaling, Metabolism, Neuroscience, Nuclear Hormone Receptors, Nuclear Receptors, Nuclear Signaling Pathways, Obesity, Signal Transduction, Signaling Pathway, Transcription, Tumor Biomarkers, Zinc Finger
*You can search these to find other products in these research areas.
|Background||Estrogen receptor-beta (ESR2) is a member of the superfamily of nuclear receptors, which can transduce extracellular signals into transcriptional responses. 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.|
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,