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07-697-25UL
Sigma-AldrichAnti-E-Cadherin
Detect E-Cadherin using this Anti-E-Cadherin Antibody validated for use in Immunohistochemistry and WB.
More>>Detect E-Cadherin using this Anti-E-Cadherin Antibody validated for use in Immunohistochemistry and WB. Less<<
Anti-E-Cadherin: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Cadherin-1 (UniProt: P12830; also known as CAM 120/80, Epithelial cadherin, E-cadherin, Uvomorulin, CD324) is encoded by the CDH1 (also known as CDHE, UVO) gene (Gene ID: 999) in human. Cadherins are calcium-dependent cell adhesion molecules that participate in cell-cell adhesion during embryogenesis, development, organogenesis, and differentiation. E-cadherin is a single-pass type I membrane glycoprotein that is mainly expressed in non-neural epithelial tissues. It is synthesized with a signal peptide (aa 1-22) and a propeptide (aa 23-154) that are subsequently cleaved off to produce the mature form that contains an extracellular domain (aa 155-709), a transmembrane domain (aa 710-730), and a cytoplasmic domain (aa 731-882). N-glycosylation at Asn-637 is shown to be essential for its expression, folding, and trafficking. E-cadherin is known to contain five cadherin domains. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. Post-translationally it can be cleaved into three chains: E-Cad/CTF1 (aa 701-882); E-Cad/CTF2 (aa 732-882); and E-Cad/CTF3 (aa 751-882). During apoptosis or with calcium influx, it is cleaved by a membrane-bound metalloproteinase (ADAM10; at residues 700-701), which causes disruption of cell-cell adhesion and the subsequent release of b-catenin into the cytoplasm. The residual membrane-tethered cleavage product is then rapidly degraded via an intracellular proteolytic pathway. It can also be cleaved by PS1/g-secretase (at residues 731-732) and this cleavage promotes disassembly of adherens junctions. Caspase 3 can cleave it at residues 750-751, which releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. (Ref.: Marambaud, M., et al. (2002). EMBO J. 21(8); 1948-1956; Steinhausen, U., et al. (2001). J. Biol. Chem. 276(7); 4972-4980; Ito, K., et al. (1999). Oncogene. 18(50); 7080-7090).
This gene is a classical cadherin from the cadherin superfamily. 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. Mutations in this gene are correlated with gastric, breast, colorectal, thyroid and ovarian cancer. Loss of function is thought to contribute to progression in cancer by increasing proliferation, invasion, and/or metastasis. The ectodomain of this protein mediates bacterial adhesion to mammalian cells and the cytoplasmic domain is required for internalization. Identified transcript variants arise from mutation at consensus splice sites.
FUNCTION: SwissProt: P12830 # E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. SIZE: 882 amino acids; 97456 Da SUBUNIT: Homodimer; disulfide-linked. Interacts directly, via the cytoplasmic domain, with CTNNB1 or JUP to form the PSEN1/cadherin/catenin adhesion complex which connects to the actin skeleton through the actin binding of alpha-catenin. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLG7. SUBCELLULAR LOCATION: Cell junction. Cell membrane; Single-pass type I membrane protein. Note=Colocalizes with DLG7 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. TISSUE SPECIFICITY: Non-neural epithelial tissues. PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm. The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway. Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. The gamma-secretase-mediated cleavage promotes disaaaembly of adherens junctions. DISEASE: "SwissProt: P12830 # Defects in CDH1 are involved in dysfunction of the cell- cell adhesion system, triggering cancer invasion (gastric, breast, ovary, endometrium and thyroid) and metastasis. & Defects in CDH1 are a cause of hereditary diffuse gastric cancer (HDGC) [MIM:137215]. & Defects in CDH1 are a cause of susceptibility to endometrial cancer [MIM:608089]." SIMILARITY: SwissProt: P12830 ## Contains 5 cadherin domains.
Molecular Weight
106kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Routinely evaluated by immunoblot with RIPA lysates from HepG2 cells.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
