bs-70366R

DATASHEET

Host: Rabbit

Target Protein: Unphosphorylated N-Cadherin (Tyr-820)

Specificity: 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.

Modification Site: Tyr-820

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P19022

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

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

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.