|Detection of VE‑Cadherin in HUVEC Human Cells by Flow Cytometry. HUVEC human umbilical vein endothelial cells were stained with Mouse Anti-Human VE‑Cadherin APC‑conjugated Monoclonal Antibody (Catalog # FAB9381A, filled histogram) or isotype control antibody (Catalog # IC0041A, open histogram). Cells were stained in a buffer containing Ca2+ and Mg2+. View our protocol for Staining Membrane-associated Proteins.|
Vascular Endothelial (VE)-Cadherin (VE-CAD), also called 7B4 and Cadherin‑5 (CDH5), is a member of the cadherin family of cell adhesion molecules. Cadherins are calcium-dependent transmembrane proteins which bind to one another in a homophilic manner. On their cytoplasmic side, they associate with the three catenins, alpha, beta, and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Without association with the catenins, the cadherins are non-adhesive. Cadherins play a role in development, specifically in tissue formation. They may also help to maintain tissue architecture in the adult. VE-Cadherin has been shown to play important roles in vasculogenesis and angiogenesis. VE-Cadherin is a classical cadherin molecule. Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating calcium-dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. Human VE-Cadherin is a 784 amino acid (aa) residue protein with a 25 aa signal sequence and a 759 aa propeptide. The mature protein begins at amino acid 48 and has a 546 aa extracellular domain, a 27 aa transmembrane domain, and a 164 aa cytoplasmic domain. The human and mouse mature VE-Cadherin proteins share approximately 74% homology.