Estrogen Receptor alpha (phospho-Tyr-537) Blocking Peptide
€155.00
In stock
SKU
ECM-EX5475
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.
Sequence: Phospho-ERα (Tyr-537) synthetic peptide 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 peptide is specifically recognized by ERα (Tyr-537) phospho-specific antibody (EP5471) in ELISA, and has been shown to block the reactivity of EP5471 in Western blot. In addition, the peptide is recommended for use in blocking EP5471 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Sequence: Phospho-ERα (Tyr-537) synthetic peptide 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 peptide is specifically recognized by ERα (Tyr-537) phospho-specific antibody (EP5471) in ELISA, and has been shown to block the reactivity of EP5471 in Western blot. In addition, the peptide is recommended for use in blocking EP5471 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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