Cadherins are a family of transmembrane glycoproteins involved in the Ca2+- dependent cell-cell adhesion that occurs in many tissues. These
proteins are similar in their domain structure (45-74% amino acid conservation), Ca2+ and protease-sensitivity, and molecular weight.
Cadherin-5 (VE-Cadherin or CD144) is one of a number of cadherins (cadherin-4 through -11) whose cDNAs were isolated from rat brain and
retina. These cadherins have a cytoplasmic domain that is highly conserved relative to previously identified cadherins, indicating that this
domain is essential for cell adhesion activity. This function is mediated by cadherin interaction with cytoskeletal proteins. However,
Cadherin-5's cytoplasmic domain has the lowest degree of homology with the other cadherins. Cadherin-5 is expressed in brain and various
other tissues, including umbilical cord vein endothelial cells. A new type of adhering junction has been identified in certain vascular
endothelial cells. These junctions are known as "complexus adherens" and are morphologically and compositionally distinct from desmosomes
and zonula adherens junctions. The complexus adherens of endothelial cells lack desmosomal cadherins as well as E-Cadherin. However,
these cells are rich in Cadherin-5 which colocalizes with desmoplakin and γ-Catenin (plakoglobin).
原厂资料:
注意事项:
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.