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Western blot analysis of E-Cadherin on A431 cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-E-Cadherin.
Immunofluorescent staining of Human Fibroblast cells with anti-E-Cadherin antibody.
BD Transduction Laboratories™ Purified Mouse Anti-E-Cadherin
BD Transduction Laboratories™ Purified Mouse Anti-E-Cadherin
Regulatory Statusの凡例
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation and Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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 a critical regulator of epithelial junction formation. Its association with catenins is necessary for cell-cell adhesion. These E-cadherin/catenin complexes associate with cortical 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.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Behrens J, Vakaet L, Friis R, et al. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature-sensitive v-SRC gene.. J Cell Biol. 1993; 120(3):757-66. (Biology). View Reference
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Chitaev NA, Troyanovsky SM. Adhesive but not lateral E-cadherin complexes require calcium and catenins for their formation. J Cell Biol. 1998; 142(3):837-846. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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Huan Y, van Adelsberg J. Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins. J Clin Invest. 1999; 104(10):1459-1468. (Clone-specific: Immunohistochemistry, Western blot). View Reference
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Takeichi M. The cadherins: cell-cell adhesion molecules controlling animal morphogenesis.. Development. 1988; 102(4):639-55. (Biology). View Reference
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Zundel W, Swiersz LM, Giaccia A. Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide. Mol Cell Biol. 2000; 20(5):1507-1514. (Clone-specific: Western blot). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.