Back to Previous Page

Anti-phospho-VE-Cadherin (Tyr685) Antibody, Alexa Fluor(R) 555 Conjugate from rabbit, ALEXA FLUOR(R) 555

ITEM#: 3042-ABT1760AF555

MFR#: ABT1760-AF555

Cadherin-5 (UniProt P33151; also known as 7B4 antigen, CD144, Vascular endothelial cadherin, VE-Cad, VE-cadherin) is encoded by the CDH5 gene (Gene ID 1003) in human. Cadherins (calcium-dependent adhesion) are type-1 transmembrane proteins that form

Cadherin-5 (UniProt P33151; also known as 7B4 antigen, CD144, Vascular endothelial cadherin, VE-Cad, VE-cadherin) is encoded by the CDH5 gene (Gene ID 1003) in human. Cadherins (calcium-dependent adhesion) are type-1 transmembrane proteins that form adherens junctions in tissues and play important roles in mediating cell adhesion. Cadherins are designated with a prefix that specifies their tissue association. Vascular endothelial-cadherin (VE-cadherin) is the transmembrane component of the endothelial adherens junction between vascular endothelial cells (ECs) and plays a pivotal role in endothelium integrity and in the control of vascular permeability. One characteristic of VEGF-induced vascular permeability is the phosphorylation of VE-cadherin by Src family kinases (SFK), which leads to VE-cadherin internalization and the destabilization of adherens junctions. Likewise, VE-cadherin overexpression is shown to decrease the permeability of endothelial monolayers in vitro. SFK activation by dominant negative Csk overexpression is reported to result in VE-cadherin phosphorylation at tyrosines 658, 685, and 731 in human dermal microvascular endothelial cells (HDMECs) without affecting HDMEC monolayer permeability. On the other hand, expression of constitutively active Src promoted VE-cadherin phosphorylation on tyrosines 658 and 731 and decreased barrier function, suggesting that concurrent signaling events in addition to VE-cadherin tyrosine phosphorylation are needed to promote barrier permeability in response to inflammatory mediators or growth factors. VE-cadherin is initially produced with a signal peptide (a.a. 1-24) and a propeptide (a.a. 25-45) sequence, the removal of which yields tthe mature protein containing a large extracellular region (a.a. 46-599) with five cadherine repeats (a.a. 46-149, 150-256, 257-371, 372-476, 477-593), followed by a transmembrane segment (a.a. 600-620) and a cytoplasmic domain (a.a. 621-784).