產(chǎn)品編號(hào) | bs-3130P |
英文名稱 | Phospho-ESR1 (Ser118) Antibody Blocking Peptide |
中文名稱 | 磷酸化雌激素受體α封閉多肽 |
別 名 | Estrogen Receptor alpha (phospho S118); p-Estrogen Receptor alpha (phospho S118); ER (phospho S118); p-ER (phospho S118); ER alpha (Phospho-Ser118); ER alpha (Phospho-S118); Phospho-ER alpha (S118); ; Phospho-ER alpha (Ser118); p-ER alpha (Ser118); p-ER alpha (S118); Phospho-Estrogen Receptor alpha (S118); Phospho-Estrogen Receptor alpha (S118); Estradiol receptor; Estrogen receptor alpha; Estradiol Receptor-alpha; Estrogen Receptor 1; Atherosclerosis, susceptibility to, included; DKFZp686N23123; ER Alpha; ER; ER-alpha; ERalpha; ER[a]; Era; ESR; ESR1; ESR1_HUMAN; ESR2; ESRA; Estr; Estrogen receptor 1 (alpha); Estrogen resistance, included; HDL cholesterol, augmented response of, to hormone replacement, included; Myocardial infarction, susceptibility to, included; NR3A1; Nuclear receptor subfamily 3 group A member 1; OTTHUMP00000017718; OTTHUMP00000017719; RNESTROR. |
性 狀 | Lyophilized powder |
物 種 | human |
純化方法 | HPLC |
活性 | Not tested |
保存條件 | Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
注意事項(xiàng) | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
產(chǎn)品介紹 | Estrogen and progesterone receptor are members of a family of transcription factors that are regulated by the binding of their cognate ligands. The interaction of hormone-bound estrogen receptors with estrogen responsive elements(EREs) alters transcription of ERE-containing genes. The carboxy terminal region of the estrgen receptor contains the ligand binding domain, the amino terminus serves as the transactivation domain, and the DNA binding domain is centrally located. Two forms of estrogen receptor have been identified, ER alpha and ER beta. ER alpha and ER beta have been shown to be differentially activated by various ligands. The biological response to progesterone is mediated by two distinct forms of the human progesterone receptor (hPR-A and hPR-B), which arise from alternative splicing. In most cells, hPR-B functions as a transcriptional activator of progesterone-responsive gene, whereas hPR-A function as a transcriptional inhibitor of all steroid hormone receptors. Function : Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Isoform 3 can bind to ERE and inhibit isoform 1. SWISS: P03372 Gene ID: 2099 |
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