Beta-Catenin (N-terminal) Blocking Peptide
€155.00
In stock
SKU
ECM-CX1065
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 654 in the C-terminal armadillo repeat of β-Catenin. This phosphorylation regulates β-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of β-Catenin may regulate specific protein-protein interactions leading to changes in cell adhesion.
Sequence: β-Catenin synthetic peptide corresponding to amino acid residues in the N-terminal region of human β-Catenin. This human sequence is highly conserved in rat and mouse β-Catenin.
Specificity: The peptide is specifically recognized by anti-β-Catenin (N-terminal) antibody (CP1061) in ELISA, and is recommended for use in blocking CP1061 reactivity in Western blot and 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 654 in the C-terminal armadillo repeat of β-Catenin. This phosphorylation regulates β-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of β-Catenin may regulate specific protein-protein interactions leading to changes in cell adhesion.
Sequence: β-Catenin synthetic peptide corresponding to amino acid residues in the N-terminal region of human β-Catenin. This human sequence is highly conserved in rat and mouse β-Catenin.
Specificity: The peptide is specifically recognized by anti-β-Catenin (N-terminal) antibody (CP1061) in ELISA, and is recommended for use in blocking CP1061 reactivity in Western blot and 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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