Monkey sVE-cadherin Matched Antibody Pairs

Description: Each Module Set is sufficient for ten 96-well microtiter plates and are identical to eBioscience high quality ready-to-use Conventional ELISAs.

Cadherin-5, though member of the family of cadherins has been shown to be functionally as well as structurally distinct from classical cadherins (e.g. E-, N-, P-cadherins). Through its function and location cadherin-5 has been named VE-cadherin. Its a protein of a relative molecular mass of about 130 kDa.

The vascular endothelial cadherin (VE-cadherin) gene encodes a Ca2+-dependent cell adhesion molecule required for the organization of interendothelial junctions. VE-cadherin mediates homophilic, calcium-dependent aggregation and cell-to-cell adhesion. In addition, it decreases intercellular permeability to high-molecular weight molecules and reduces cell migration rate across a wounded area. VE-cadherin is a transmembrane protein, the intracellular domain has been shown to interact with cytoplasmic proteins called catenins that transmit the adhesion signal upon this activation. So the VE-cadherin extracellular domain is enough for early steps of cell adhesion and recognition. However, interaction of VE-cadherin the cytoskeleton, mediated through the cytoplasmatic domain, is necessary to provide strength and cohesion to the junction.

The initiation of endothelial apoptosis correlates with cleavage and disassembly of components of adherens junctions. The extracellular portion of these junctions is altered during apoptosis because VE-cadherin dramatically decreases on the surface of cells. An extracellular fragment of VE-cadherin can be detected. This shedding of VE-cadherin can be blocked by an inhibitor of metalloproteinases. It may be part of a concerted mechanism to disrupt structural and signaling properties of adherens junctions and may actively interrupt extracellular signals required for endothelial cell survival.

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