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VE-Cadherin (F4K3Y) Rabbit Monoclonal Antibody #60787

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  • WB
  • IP
  • IHC
  • IF

    Product Specifications

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 130-140
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Simple Western™ 1:10 - 1:50
    Immunoprecipitation 1:100
    Immunohistochemistry (Paraffin) 1:50 - 1:200
    Immunofluorescence (Frozen) 1:300
    Immunofluorescence (Immunocytochemistry) 1:600

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    VE-Cadherin (F4K3Y) Rabbit mAb recognizes endogenous levels of total VE-cadherin protein. Based on the sequence of the peptide antigen, this antibody is not expected to detect other cadherin family members. This antibody detects an approximately 30 kDa protein of unknown identity in some cell lines. Nonspecific labeling in fixed frozen mouse brain has been observed by immunofluorescence.

    Species Reactivity:

    Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro696 of mouse VE-cadherin protein.

    Background

    Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

    Alternate Names

    7B4; 7B4/cadherin-5; AA408225; CADH5; cadherin 5; Cadherin-5; Cd144; Cdh5; Vascular endothelial cadherin; VE-C; VE-Cad; VE-cadherin; Vec; VEcad; VECD

    For Research Use Only. Not for Use in Diagnostic Procedures.
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