Estrogen Receptor alpha (Tyr-537), phospho-specific polyclonal, anti-human, mouse, rat, chicken, frog

Background:
Estrogen receptor α (ERα) is a member of the steroid receptor superfamily and its structure includes highly conserved DNA binding and ligand binding domains found in this family. ERα regulates transcription at estrogen response elements by recruiting co-activator proteins and transcription proteins via its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively). 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 is phosphorylated by c-Src leading to nuclear export of ERα and degradation. Thus, a variety of phosphorylation events control ERα activity.

Immunogen: Phospho-ERα (Tyr-537) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Tyr-537 in human ERα. This sequence is well conserved in rat and mouse ERα, and is also well conserved in ERβ (Tyr-488).

Specificity: The antibody was cross absorbed 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 form 66 to 35 kDa* on SDS-PAGE immunoblots of MCF-7 cells treated with pervanadate, and this reactivity is removed after akaline phosphatase treatment.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.