Unphosphorylated N-Cadherin (Tyr-820) Antibody

Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886. Phosphorylation of Tyr-860 can disrupt cadherin binding to β-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.

Unphosphorylated N-Cadherin (Tyr-820) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 820 in human N-cadherin.

This antibody was cross-adsorbed to phospho-N-cadherin (Tyr-820) peptide before affinity purification using unphosphorylated N-cadherin (Tyr-820) peptide. The purified antibody detects a strong band at 130 kDa* in western blots of whole antiserum-starved human endothelial cells, but is decreased in pervanadate treated cells.