Ve-Cadherin (CDH5) Antibody – Rabbit Polyclonal

This gene is a classical cadherin from the cadherin superfamily and is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. An alternative splice variant has been described but its full length sequence has not been determined. [provided by RefSeq]

Function: Cadherins are calcium dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction. Ref.9

Subunit structure: Interacts via cadherin 5 domain with PTPRB

By similarity. Interacts with TRPC4. Interacts with KRIT1. Ref.8 Ref.9

Subcellular location: Cell junction. Cell membrane; Single-pass type I membrane protein

Probable. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Ref.9

Tissue specificity: Endothelial tissues and brain.

Post-translational modification: Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB

By similarity. Ref.7

Sequence similarities: Contains 5 cadherin domains.