Estrogen receptor α (ERα, ER; NR3A1), a member of the steroid hormone receptor family, is a ligand-activated transcription factor. ERα contains DNA binding and ligand binding domains and is expressed in various tissues, including the ovary, uterus, breast, prostate, testis, epididymis, bones, bladder, kidney, heart, vessel wall, pituitary gland, and hypothalamus. ER plays crucial roles in maintaining the reproductive, cardiovascular, musculoskeletal, and central nervous systems. Its natural ligand, 17β-estradiol, is a classical estrogenic compound. Binding of estrogen to ER induces conformational changes, triggering events like dissociation from heat shock proteins, receptor dimerization, phosphorylation, and association of the hormone-activated receptor with specific regulatory elements in target genes.
Supplied at a concentration of 1mg/ml in PBS buffer after reconstitution.
LSERASC1.
ERα consists of several functional domains:
Phosphorylation is a key regulatory mechanism for ERα activity. Several serine residues, including Ser104, Ser106, Ser118, and Ser167, are phosphorylated by different kinases, which modulate the receptor’s transcriptional activity . For instance, Ser118 is phosphorylated by CDK7, and Ser167 is phosphorylated by p90RSK and Akt . Phosphorylation at Ser167 has been associated with tamoxifen resistance in breast cancer patients .
Mouse anti-human ERα antibodies are monoclonal antibodies produced by immunizing mice with a synthetic peptide corresponding to residues surrounding Ser118 of human ERα . These antibodies are highly specific and do not cross-react with estrogen receptor beta or other family members . They are commonly used in various scientific applications, including Western blotting, immunohistochemistry, and immunocytochemistry .
Mouse anti-human ERα antibodies are valuable tools in research and clinical diagnostics. They are used to: