N-Cadherin (C-terminal region) 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 synthetic peptide (coupled to carrier protein) corresponding to amino acids from the C-terminal region of human N-cadherin.

The purified antibody detects a band at 130 kDa* in western blots of human endothelial cells and mouse brain tissue, and does not cross-react with E-cadherin. The antibody also works for ELISA, immunoprecipitation, and immunocytochemistry. This sequence is conserved in rat and mouse N-cadherin, and has three amino acid differences from the conserved region in R-cadherin.