VE-Cadherin/CD144 Polyclonal Antibody

VE-cadherin, also known as CD144, is a type II classical cadherin and member of the cadherin superfamily of calcium-dependent cell adhesion molecules.¹ It is composed of an N-terminal signal peptide, a pro-peptide, five extracellular cadherin repeats that bind to homotypic cadherins, a transmembrane domain, and a cytoplasmic tail that interacts with the cytoskeleton. VE-cadherin is endothelial cell-specific and is localized to intracellular junctions where it participates in vascular structure assembly.^2,3,4 An anti-VE-cadherin antibody in combination with an anti-CD31 antibody inhibits tube formation in human umbilical vein endothelial cells (HUVECs).⁵ Knockout of Cdh5, the gene encoding VE-cadherin, in mouse embryonic stem cells prevents the formation of vessel-like structures in 11-day-old embryoid bodies.³ VE-cadherin is overexpressed in melanoma and breast cancer and is positively correlated with poor prognosis.⁶ Cayman's VE-Cadherin/CD144 Polyclonal Antibody can be used for immunocytochemistry (ICC), immunohistochemistry (IHC), immunoprecipitation (IP), and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Yu, W., Yang, L., Li, T., et al. Cadherin signaling in cancer: Its functions and role as a therapeutic target. Front Oncol. 9, 989 (2019).

2. Lampugnani, M.G., Resnati, M., Raiteri, M., et al. A novel endothelial-specific membrane protein is a marker of cell-cell contacts. J. Cell Biol. 118(16), 1511-1522 (1992).

3. Vittet, D., Buchou, T., Schweitzer, A., et al. Targeted null-mutation in the vascular endothelial-cadherin gene impairs the organization of vascular-like structures in embryoid bodies. Proc. Natl. Acad. Sci. USA 94(12), 6273-6278 (1997).

4. Breviario, F., Caveda, L., Corada, M., et al. Functional properties of human vascular endothelial cadherin (7B4/cadherin-5), an endothelium-specific cadherin. Arterioscler. Thromb. Vasc. Biol. 15(8), 1229-1239 (1995).

5. Matsumura, T., Wolff, K., and Petzelbauer, P. Endothelial cell tube formation depends on cadherin 5 and CD31 interactions with filamentous actin. J. Immunol. 158(7), 3408-3416 (1997).

6. Bartolomé, R.A., Torres, S., Isern de Val, S., et al. VE-cadherin RGD motifs promote metastasis and constitute a potential therapeutic target in melanoma and breast cancers. Oncotarget 8(1), 215-227 (2017).

Oskolkova, O.V., Hodzic, A., Karki, P., et al. Oxidized phospholipids on alkyl-amide scaffold demonstrate anti-endotoxin and endothelial barrier-protective properties. 174, 264-271 (2021).

Ganesan, M.K., Finsterwalder, R., Leb, H., et al. Three-dimensional coculture model to analyze the cross talk between endothelial and smooth muscle cells. Tissue Eng. Part C Methods 23(1), 38-49 (2017).

Dorland, Y.L., Malinova, T.S., van Stalborch, A.M., et al. The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions. Nat. Commun. 7, 12210 (2016).