E-Cadherin is a 120kDa transmembrane glycoprotein that is localized in the adherens junctions of epithelial cells. There, it interacts with the cytoskeleton through the associated cytoplasmic catenin proteins. In addition to being a calcium-dependent adhesion molecule, E-Cadherin is also a critical regulator of epithelial junction formation. Its association with catenins is necessary for cell-cell adhesion. These E-cadherin/catenin complexes associate with corical actin bundles at both the zonula adherens and the lateral adhesion plaques. Tyrosine phosphorylation can disrupt these complexes, leading to changes in cell adhesion properties. E-Cadherin expression is often down-regulated in highly invasive, poorly differentiated carcinomas. Increased expression of E-Cadherin in these cells reduces invasiveness. Thus, loss of expression or function of E-Cadherin appears to be an important step in tumorigenic progression.
Immunofluorescence, Immunohistochemistry, Immunoprecipitation
|Human E-Cadherin aa. 735-883|
|CD324; CDH1; CADH1; Cadherin-1; ECAD; CDHE; Arc-1; LCAM; UVO; Uvomorulin|
|Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.|
|Store undiluted at -20°C.|
For Research Use Only.
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