Beta-Catenin (phospho-Tyr-86) Blocking Peptide
€155.00
In stock
SKU
ECM-CX1195
Background:
β-Catenin is a 92 kDa protein that binds to the cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions. Deletions in the cytoplasmic domain of E-Cadherin eliminate catenin binding and result in a loss of cell adhesion. Tyrosine phosphorylation of β-Catenin can regulate its interaction with critical components of adherens junctions. Both Fer and Fyn kinases phosphorylate tyrosine 142 in vitro. Overexpression of these kinases in epithelial cells disrupts interactions between α- and β-Catenins. The phosphorylation of tyrosine 142 may act as a switch from the transcriptional to the adhesive role of β-Catenin. Src family kinases can also phosphorylate tyrosine 86 and 654 in β-Catenin. The Tyr-654 phosphorylation regulates β-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of β-Catenin may regulate protein-protein interactions, leading to changes in cell adhesion.
Sequence: Phospho-β-Catenin (Tyr-86) synthetic peptide corresponds to amino acid residues around tyrosine 86 of human β-Catenin. This peptide sequence is highly conserved in rat and mouse β-Catenin.
Specificity: The peptide is specifically recognized by anti-β-Catenin (Tyr-86) phospho-specific antibody (CP1191) in ELISA, and has been shown to block the reactivity of CP1191 during Western blot. In addition, the peptide is recommended for use in blocking CP1191 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.
β-Catenin is a 92 kDa protein that binds to the cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions. Deletions in the cytoplasmic domain of E-Cadherin eliminate catenin binding and result in a loss of cell adhesion. Tyrosine phosphorylation of β-Catenin can regulate its interaction with critical components of adherens junctions. Both Fer and Fyn kinases phosphorylate tyrosine 142 in vitro. Overexpression of these kinases in epithelial cells disrupts interactions between α- and β-Catenins. The phosphorylation of tyrosine 142 may act as a switch from the transcriptional to the adhesive role of β-Catenin. Src family kinases can also phosphorylate tyrosine 86 and 654 in β-Catenin. The Tyr-654 phosphorylation regulates β-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of β-Catenin may regulate protein-protein interactions, leading to changes in cell adhesion.
Sequence: Phospho-β-Catenin (Tyr-86) synthetic peptide corresponds to amino acid residues around tyrosine 86 of human β-Catenin. This peptide sequence is highly conserved in rat and mouse β-Catenin.
Specificity: The peptide is specifically recognized by anti-β-Catenin (Tyr-86) phospho-specific antibody (CP1191) in ELISA, and has been shown to block the reactivity of CP1191 during Western blot. In addition, the peptide is recommended for use in blocking CP1191 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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