Anti-α1-Catenin (N-terminal region) Antibody

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.

Our α1-Catenin (N-terminal region) rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects chicken, human, mouse, and rat α1-Catenin (N-terminal region) and is antigen affinity purified. It is great for use in WB.

α1-Catenin synthetic peptide (coupled to KLH) corresponding to amino acid residues from the N-terminal region of 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.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.