Catalog # EP5471
Estrogen Receptor α (Tyr-537), phospho-specific
Size 100 μl
Species Reactivity Hu, Rt, Ms, Ck, Fr
MW 68 kDa
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.
Castoria, G. et al. (2012) Oncogene. 31:4868.
*For more information, see UniProt Accession P03372
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: