The cadherins are a family of Ca 2+-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins each contain a large extracellular domain at the amino-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short carboxy-terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including beta-catenin, to regulate cadherin function. VE-cadherin (for vascular endothelial cadherin, also designated cadherin-5) is localized at intercellular junctions of endothelial cells, where it is thought to play a role in the cohesion and organization of intercellular junctions.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
p-VE-Cadherin (Y731) polyclonal antibody detects endogenous levels of VE-Cadherin protein only when phosphorylated at Tyr731
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