Alpha1-Catenin (a.a. 143-153) Blocking Peptide
€155.00
In stock
SKU
ECM-CX3435
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: α1-Catenin synthetic peptide corresponds to amino acid residues 143 to 153 in human α1-Catenin. This peptide sequence is highly conserved in rat and mouse α1-Catenin, and has some homology to α2-Catenin or α3-Catenin.
Specificity: The peptide is specifically recognized by α1-Catenin (a.a. 143-153) (CP3431) in ELISA, and has been shown to block the reactivity of CP3431 in Western blot. In addition, the peptide is recommended for use in blocking CP3431 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: α1-Catenin synthetic peptide corresponds to amino acid residues 143 to 153 in human α1-Catenin. This peptide sequence is highly conserved in rat and mouse α1-Catenin, and has some homology to α2-Catenin or α3-Catenin.
Specificity: The peptide is specifically recognized by α1-Catenin (a.a. 143-153) (CP3431) in ELISA, and has been shown to block the reactivity of CP3431 in Western blot. In addition, the peptide is recommended for use in blocking CP3431 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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