ER-beta1 (Estrogen Receptor b

分子量：
53-59kDa
细胞定位：
Antigen Cellular Localization: Nucleus {ECO:0000255|PROSITE- ProRule:PRU00407, ECO:0000269|PubMed:19126643}
形式：
Liquid. In PBS containing 0.02% sodium azide.
参考文献：
Skliris GP et. al. J Pathol 2002;197:155-62. |
产品概述：
We constantly strive to ensure we provide our customers with the best antibodies. As a result of this work we offer this antibody in purified format. We are in the process of updating our datasheets. If you have any questions regarding this update, please feel free to contact our technical support team. This product is a high quality ER-beta1 (Estrogen Receptor beta-1) antibody.
功能：
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.
总结：
Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ER-alpha and ER-beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. They are located in the nucleus, though some estrogen receptors associate with the cell surface membrane and can be rapidly activated by exposure of cells to estrogen. ER-alpha and ER-beta are differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER-alpha and ER-beta may be regulated by distinct mechanisms even though they share many functional characteristics.
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