Estrogen Receptor α (Tyr-537), Phosphospecific Antibody

Applications

Reactivity

Human
Mouse
Rat
Chicken
Xenopus

Overview
Catalog #	bs-70493r-100ul
Product Name	Estrogen Receptor α (Tyr-537), Phosphospecific Antibody
Applications	WB
Specificity	The antibody was cross-adsorbed to unphosphorylated ERα (Tyr-537) peptide before affinity purification using phospho-ERα (Tyr-537) peptide (without carrier). This antibody detects several forms of ERα ranging from 66 to 35 kDa* on SDS-PAGE immunoblots of MCF-7 cells treated with pervanadate, and this reactivity is removed after alkaline phosphatase treatment. This sequence is well conserved in rat and mouse ERα, and is also well conserved in ERβ (Tyr-488).
Reactivity	Human, Mouse, Rat, Chicken, Xenopus
Specifications
Conjugation	Unconjugated
Host	Rabbit
Source	Phospho-ERα (Tyr-537) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Tyr-537 in human ERα.
Modification Site	Tyr-537
Clonality	Polyclonal
Isotype	IgG
Purification	Antigen Affinity purification
Storage Buffer	PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Storage Condition	Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Target
Swiss Prot	P03372
Synonyms	ESR, ESR1, ESRA, Estradiol receptor, Eralpha, ER
Background	Estrogen receptor α (ERα) is a member of the steroid receptor superfamily and its structure includes an N-terminal ligand-independent transactivation domain (AF-1), a highly conserved DNA binding domain, and a C-terminal ligand-dependent transactivation domain (AF-2). AF-1 and AF-2 activate transcription independently and synergistically, and act in a promoter- and cell-specific manner. Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity. Ser-104, Ser-106, Ser-118, and Ser-167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. In addition to these sites, phosphorylation of Tyr-537 has been implicated in maximal hormone binding, dimerization, and transcriptional activity. Tyr-537, located in the AF-2 domain, is phosphorylated by c-Src leading to nuclear export of ERα and degradation. Thus, a variety of phosphorylation events control ERα activity.
Application Dilution
WB	1:300-5000