Cell Signaling Technology

Product Pathways - Adhesion

VE-Cadherin Antibody #2158

Applications Reactivity MW (kDa) Source
W IP IF-IC H B 130-140 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  B=Bovine
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

VE-Cadherin Antibody detects endogenous levels of total VE-cadherin protein. The antibody does not cross-react with other cadherin family members.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to the carboxy-terminus of human VE-cadherin. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types, using VE-Cadherin Antibody.

IP

IP

Immunoprecipitation of VE-Cadherin from human umbillical vein endothelial cell (HUVEC) lysates, using VE-Cadherin Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of HUVE cells, using VE-Cadherin Antibody (green) and MEK1/2 (L38C12) Mouse mAb #4694 (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).


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 which are found in adherens junctions (AJ), 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). Unlike β- and γ-catenin, p120 regulates cadherin adhesive activity and trafficking rather than having a structural role in the junctional complex (1-4). E-cadherin is considered an acting suppressor of invasion and growth of many epithelial cancers (1-3). Recent 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 over-expression of MMP-9 and cellular invasion (3). In endothelial cells, VE-cadherin signaling, expression and localization are correlated with vascular permeability and tumor angiogenesis (5,6). Expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

  1. Wheelock, M.J. and Johnson, K.R. (2003) Annu. Rev. Cell. Dev. Biol. 19, 207-235.
  2. Christofori, G. (2003) EMBO J. 22, 2318-2323.
  3. Hazan, R.B. et al. (2004) Ann. NY Acad. Sci. 1014, 155-163.
  4. Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol. 14, 427-434.
  5. Rabascio, C. et al. (2004) Cancer Res. 64, 4373-4377.
  6. Yamaoka-Tojo, M. et al. (2006) Arterioscler. Thromb. Vasc. Biol. 26, 1991-1997.
  7. Patel, I.S. et al. (2003) Int. J. Cancer 106, 172-177.
  8. Sanders, D.S. et al. (2000) J. Pathol. 190, 526-530.

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