Estrogen Receptor alpha Antibody (YA5938),MedChemexpress,HY-P86246

ESR1 is a nuclear hormone receptor involved in regulating eukaryotic gene expression and affecting cellular proliferation and differentiation in target tissues. Its ligand-dependent nuclear transactivation involves direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors (e.g., AP-1/c-Jun, c-Fos, ATF-2, Sp1, and Sp3) to mediate ERE-independent signaling. Ligand binding induces a conformational change, enabling combinatorial association with multiprotein coactivator complexes through LXXLL motifs. ESR1 and NF-kappa-B mutually repress each other in a cell-type-specific manner, reducing NF-kappa-B DNA-binding activity and inhibiting NF-kappa-B-mediated transcription from the IL6 promoter while displacing RELA/p65 and coregulators. ESR1 is recruited to the NF-kappa-B response elements of CCL2 and IL8 promoters, displacing CREBBP. It coexists with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences and can synergize with NF-kappa-B to activate transcription via adjacent response element recruitment, a process requiring CREBBP. ESR1 also activates TFF1 transcriptional activity and mediates membrane-initiated estrogen signaling involving kinase cascades. It is essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (PubMed:17922032). In the presence of circulating estradiol (17-beta-estradiol/E2), ESR1 maintains neuronal survival during ischemic reperfusion injury (By similarity) and is involved in NOS3 activation and endothelial nitric oxide production (PubMed:21937726). Isoforms lacking functional domains modulate transcriptional activity via competitive ligand/DNA binding or heterodimerization with the full-length receptor (PubMed:10970861). ESR1 binds to ERE and inhibits isoform 1 (PubMed:10970861).

ESR1 ESR NR3A1