|Detection of Human VE‑Cadherin by Western Blot. Western blot shows lysate of HUVEC human umbilical vein endothelial cells. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human VE‑Cadherin Monoclonal Antibody (Catalog # MAB9381) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for VE‑Cadherin at approximately 125 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
VE‑Cadherin in HUVEC Cells.|
VE‑Cadherin was detected in immersion fixed HUVEC cells using Mouse Anti-Human
VE‑Cadherin Monoclonal Antibody (Catalog # MAB9381) at 0.5 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to plasma membrane. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
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.
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Showing Results 1 - 2 of 2
Filter your results:
The document you requested is not available online. Please enter the Catalog Number and Lot Number below to have a document emailed to you at the address provided