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Anti-Estrogen Receptor-α (Phospho-Tyr537) Antibody

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Anti-Estrogen Receptor-α (Phospho-Tyr537) Antibody

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Anti-Estrogen Receptor-α (Phospho-Tyr537) Antibody

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Overview

Name:	Anti-Estrogen Receptor-α (Phospho-Tyr537) Antibody See all Estrogen Receptor-α primary antibodies
Description:	Rabbit polyclonal antibody to Estrogen Receptor-α (Phospho-Tyr537)
Specificity:	The antibody detects endogenous levels of ER-α only when phosphorylated at tyrosine 537.
Applications:	WB, IHC
Dilutions:	Western blotting: 1:500~1:1000Immunohistochemistry: 1:50~1:100
Reactivity:	Human, Mouse
Immunogen:	Peptide sequence around phosphorylation site of tyrosine 537(P-L-Y(p)-D-L) derived from Human Estrogen Receptor-α.
Host:	Rabbit
Clonality:	Polyclonal
Conjugate:	Unconjugated
Purification:	Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Concentration:	1.0mg / ml
Formulation:	Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage:	Store at -20?C / 1 year

Target

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. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3. Isoform 3 can bind to ERE and inhibit isoform 1.
Tissue Specificity:	Widely expressed. Isoform 3 is not expressed in the pituitary gland.
Involvement in Disease:	Estrogen resistance: A disorder characterized by partial or complete resistance to estrogens, in the presence of elevated estrogen serum levels. Clinical features include absence of the pubertal growth spurt, delayed bone maturation, unfused epiphyses, reduced bone mineral density, osteoporosis, continued growth into ***hood and very tall *** stature. Glucose intolerance, hyperinsulinemia and lipid abnormalities may also be present.
Sequence Similarities:	Belongs to the nuclear hormone receptor family. NR3 subfamily.
Post-Translational Modification:	Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. Phosphorylated by LMTK3 in vitro.
Cellular Location:	Nucleus. Cytoplasm. Cell membrane. A minor fraction is associated with the inner membrane.