N-Cadherin (Tyr-820), phospho-specific polyclonal, anti-human, mouse, rat

Background:
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.

Immunogen: Phospho-N-Cadherin (Tyr-820) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 820 in human N-cadherin. This sequence is conserved in rat and mouse N-cadherin, and has three amino acid differences from the conserved site in R-cadherin.

Specificity: This antibody was cross-adsorbed to phospho-N-Cadherin (Tyr-860) and unphosphorylated N-cadherin (Tyr-820) peptides before affinity purification using phospho-N-cadherin (Tyr-820) peptide. The purified antibody detects a 130 kDa* band corresponding to N-cadherin in western blots of serum-starved human endothelial cells treated with pervanadate, but is not detected in untreated cells.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.