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This antibody was cross-adsorbed to phospho-N-Cadherin (Tyr-820) and unphosphorylated N-cadherin (Tyr-860) peptides before affinity purification using phospho-N-cadherin (Tyr-860) peptide. In western blots, the antibody detects a 130 kDa* band corresponding to N-cadherin (Tyr-860) in human endothelial cells treated with pervanadate and detects a 120 kDa band corresponding to E-cadherin (Tyr-835) in human A431 cells treated with pervanadate.
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 beta-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: cadherin 2 type 1 N-cadherin (neuronal); cadherin 2, type 1, N-cadherin (neuronal); Cadherin-2; calcium-dependent adhesion protein, neuronal; CD325; CDw325; N-cadherin; N-cadherin 1; Neural cadherin
Gene Aliases: CD325; CDH2; CDHN; CDw325; N-cadherin; NCAD
UniProt ID: (Human) P19022, (Mouse) P15116, (Rat) Q9Z1Y3
Entrez Gene ID: (Human) 1000, (Mouse) 12558, (Rat) 83501
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