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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.
- For fluorochrome spectra and suitable instrument settings, please refer to our Multicolor Flow Cytometry web page at www.bdbiosciences.com/colors.
E-Cadherin is a 120-kDa 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 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. The 36/E-Cadherin monoclonal antibody recognizes the cytoplasmic domain of E-Cadherin, regardless of phosphorylation status. The peptide immunogen was generated from human E-Cadherin aa. 735-883.
Note: Investigators are advised that this antibody has some degree of cross-reactivity to P-Cadherin.
Development References (7)
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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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Jaksits S, Kriehuber E, Charbonnier AS, Rappersberger K, Stingl G, Maurer D. CD34+ cell-derived CD14+ precursor cells develop into Langerhans cells in a TGF-beta 1-dependent manner. J Immunol. 1999; 163(9):4869-4877. (Clone-specific: Flow cytometry). View Reference
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Miyoshi K, Shillingford JM, Smith GH, et al. Signal transducer and activator of transcription (Stat) 5 controls the proliferation and differentiation of mammary alveolar epithelium. J Cell Biol. 2001; 155(4):531-542. (Clone-specific: Immunohistochemistry). View Reference
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Sheibani N, Sorenson CM, Frazier WA. Differential modulation of cadherin-mediated cell-cell adhesion by platelet endothelial cell adhesion molecule-1 isoforms through activation of extracellular regulated kinases. Mol Biol Cell. 2000; 11(8):2793-2802. (Clone-specific: Immunofluorescence, 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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Tamm I, Cardinale I, Kikuchi T, Krueger JG. E-cadherin distribution in interleukin 6-induced cell-cell separation of ductal breast carcinoma cells. Proc Natl Acad Sci U S A. 1994; 91(10):4338-4342. (Biology). View Reference
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Weng Z, Xin M, Pablo L, et al. Protection against anoikis and down-regulation of cadherin expression by a regulatable beta-catenin protein. J Biol Chem. 2002; 277(21):18677-18686. (Clone-specific: Immunofluorescence, Immunoprecipitation, 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.
