Alpha1-Catenin (phospho-Tyr-148) Blocking Peptide
€155.00
In stock
SKU
ECM-CX3455
Background:
α-catenins are cadherin interacting proteins with homology to vinculin. Three α-catenin genes have been described including α1-catenin (αE-Catenin), α2-catenin (αN-catenin), and α3-catenin (αT-catenin). α1-catenin has 81% homology with α2-catenin and 60% homology with α3-catenin. These α-catenin isoforms may have similar roles since each binds cadherins. However, their expression patterns are both overlapping and distinct. α1-catenin was identified in epithelial cells, and is expressed in various cell types. α2-catenin is enriched in the nervous system, and α3-catenin is expressed highest in testis and heart. Phosphorylation may regulate the activity of α1-catenin, since tyrosine phosphorylation of Tyr-148 occurs during intercellular adhesion. This site is dephosphorylated by SHP2, which inhibits α1-catenin binding to β-catenin and translocation to the plasma membrane. Phosphorylation of α1-catenin at Tyr-148 may be important for inhibition of cell transformation, and dephosphorylation of this site may be important during SHP2-mediated cell transformation.
Sequence: Phospho-α1-Catenin (Tyr-148) synthetic peptide corresponds to amino acid residues around tyrosine 148 in human α1-Catenin. This peptide sequence is highly conserved in rat and mouse α1-Catenin, but is not conserved in α2-Catenin or α3-Catenin.
Specificity: The peptide is specifically recognized by α1-Catenin (Tyr-148), phospho-specific antibody (CP3451) in ELISA, and has been shown to block the reactivity of CP3451 in Western blot. In addition, the peptide is recommended for use in blocking CP3451 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.
α-catenins are cadherin interacting proteins with homology to vinculin. Three α-catenin genes have been described including α1-catenin (αE-Catenin), α2-catenin (αN-catenin), and α3-catenin (αT-catenin). α1-catenin has 81% homology with α2-catenin and 60% homology with α3-catenin. These α-catenin isoforms may have similar roles since each binds cadherins. However, their expression patterns are both overlapping and distinct. α1-catenin was identified in epithelial cells, and is expressed in various cell types. α2-catenin is enriched in the nervous system, and α3-catenin is expressed highest in testis and heart. Phosphorylation may regulate the activity of α1-catenin, since tyrosine phosphorylation of Tyr-148 occurs during intercellular adhesion. This site is dephosphorylated by SHP2, which inhibits α1-catenin binding to β-catenin and translocation to the plasma membrane. Phosphorylation of α1-catenin at Tyr-148 may be important for inhibition of cell transformation, and dephosphorylation of this site may be important during SHP2-mediated cell transformation.
Sequence: Phospho-α1-Catenin (Tyr-148) synthetic peptide corresponds to amino acid residues around tyrosine 148 in human α1-Catenin. This peptide sequence is highly conserved in rat and mouse α1-Catenin, but is not conserved in α2-Catenin or α3-Catenin.
Specificity: The peptide is specifically recognized by α1-Catenin (Tyr-148), phospho-specific antibody (CP3451) in ELISA, and has been shown to block the reactivity of CP3451 in Western blot. In addition, the peptide is recommended for use in blocking CP3451 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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