Product Pathways - Adhesion
VE-Cadherin (D87F2) XP® Rabbit mAb #2500
|2500S||100 µl (10 western blots)||---||In Stock||---|
|2500P||40 µl (4 western blots)||---||In Stock||---|
|2500||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, D. melanogaster, Bovine, Pig||Endogenous||130-140||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry
Specificity / Sensitivity
VE-Cadherin (D87F2) XP® Rabbit mAb recognizes endogenous levels of total VE-cadherin protein. The antibody does not cross-react with other cadherin family proteins.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human VE-cadherin.
Western blot analysis of extracts from HUVEC and BAEC cells using VE-Cadherin (D87F2) XP® Rabbit mAb.
Immunoprecipitation of VE-caderin from HUVEC cells using VE-Cadherin (D87F2) XP® Rabbit mAb followed by western blot using the same antibody. Lane 1 is 5% input.
Confocal immunofluorescent analysis of HUVE cells (left) and HeLa cells (right) using VE-Cadherin (D87F2) XP® Rabbit mAb (green). Actin filaments have been labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).
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 up-regulated 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).
- Wheelock, M.J. and Johnson, K.R. (2003) Annu Rev Cell Dev Biol 19, 207-35.
- Christofori, G. (2003) EMBO J 22, 2318-23.
- Hazan, R.B. et al. (2004) Ann N Y Acad Sci 1014, 155-63.
- Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol 14, 427-34.
- Rabascio, C. et al. (2004) Cancer Res 64, 4373-7.
- Yamaoka-Tojo, M. et al. (2006) Arterioscler Thromb Vasc Biol 26, 1991-7.
- Patel, I.S. et al. (2003) Int J Cancer 106, 172-7.
- Sanders, D.S. et al. (2000) J Pathol 190, 526-30.
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
DRAQ5 is a registered trademark of Biostatus Limited.
XP is a registered trademark of Cell Signaling Technology, Inc.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.