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E-Cadherin/CDH1/E-cad/CD324 Protein, Antibody, ELISA Kit, cDNA Clone

Mouse E-Cadherin/CDH1/E-cad/CD324 Protein

Description: Active
Expression host: Human Cells
  • Slide 1
  • Slide 1
50671-M08H-50
50671-M08H-100
50 µg / $178
100 µg / $298
Add to Cart

Rat E-Cadherin/CDH1/E-cad/CD324 Protein

Expression host: Human Cells
  • Slide 1
80274-R02H-50
80274-R02H-100
50 µg / $178
100 µg / $298
Add to Cart
Expression host: Human Cells
  • Slide 1
80274-R08H-50
80274-R08H-100
50 µg / $178
100 µg / $298
Add to Cart

Human E-Cadherin/CDH1/E-cad/CD324 Protein

Expression host: Human Cells
  • Slide 1
10204-H02H-50
10204-H02H-100
50 µg / $138
100 µg / $248
Add to Cart
Expression host: Baculovirus-Insect Cells
  • Slide 1
10204-H08B-20
10204-H08B-100
20 µg / $98
100 µg / $248
Add to Cart
Description: Active
Expression host: Human Cells
  • Slide 1
10204-H08H-100
10204-H08H-200
100 µg / $248
200 µg / $398
Add to Cart

E-Cadherin/CDH1/E-cad/CD324 Related Areas

E-Cadherin/CDH1/E-cad/CD324 Related Pathways

E-Cadherin/CDH1/E-cad/CD324 Related Product

    E-Cadherin/CDH1/E-cad/CD324 Summary & Protein Information

    E-Cadherin/CDH1/E-cad/CD324 Background

    Gene Summary: This CDH1 gene is a classical cadherin from the cadherin superfamily. E-cadherin 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 CDH1 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 E-cadherin mediates bacterial adhesion to mammalian cells and the cytoplasmic domain is required for internalization. Identified transcript variants arise from mutation at consensus splice sites.
    General information above from NCBI
    Subunit structure: Homodimer; disulfide-linked. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha- catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F- actin by other proteins such as LIMA1. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5 (By similarity). Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1. Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with PIP5K1C. Interacts with RAB8B (By similarity). Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization.
    Domain: 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.
    Subcellular location: Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome. Golgi apparatus, trans-Golgi network. Note=Colocalizes with DLGAP5 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. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane.
    Tissue specificity: Non-neural epithelial tissues.
    Induction: Expression is repressed by MACROD1.
    Post-translational: 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 disassembly of adherens junctions.
    N-glycosylation at Asn-637 is essential for expression, folding and trafficking.
    Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754.
    Involvement in disease: Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Note=The disease is caused by mutations affecting the gene represented in this entry. Heterozygous germline mutations CDH1 are responsible for familial cases of diffuse gastric cancer. Somatic mutations has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer.
    Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Sequence similarity: Contains 5 cadherin domains.
    General information above from UniProt

    Cadherins are calcium-dependent cell adhesion proteins which preferentially interact with themselves in a homophilic manner in connecting cells, and thus may contribute to the sorting of heterogeneous cell type. E-cadherin (E-Cad), also known as CDH1 and CD324, is a calcium-dependent cell adhesion molecule the intact function of which is crucial for the establishment and maintenance of epithelial tissue polarity and structural integrity. Mutations in CDH1 occur in diffuse type gastric cancer, lobular breast cancer, and endometrial cancer. In human cancers, partial or complete loss of E-cadherin expression correlates with malignancy. During apoptosis or with calcium influx, E-Cad is cleaved by the metalloproteinase to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. E-Cad has been identified as a potent invasive suppressor, as downregulation of E-cadherin expression is involved in dysfunction of the cell-cell adhesion system, and often correlates with strong invasive potential and poor prognosis of human carcinomas.

    E-Cadherin/CDH1/E-cad/CD324 Alternative Name

    Arc-1,CD324,CDH1,CDHE,ECAD,E-Cadherin,LCAM,UVO, [human]
    AA960649,Cdh1,Ecad,E-Cadherin,L-CAM,MGC107495,Um,UVO, [mouse]

    E-Cadherin/CDH1/E-cad/CD324 Related Studies

  • Wang HD, et al. (2004) CDH1 germline mutation in hereditary gastric carcinoma. World J Gastroenterol. 10(21): 3088-93.
  • Masterson J, et al. (2007) Posttranslational truncation of E-cadherin and significance for tumour progression. Cells Tissues Organs. 185(1-3): 175-9.
  • Mrgineanu E, et al. (2008) Correlation between E-cadherin abnormal expressions in different types of cancer and the process of metastasis. Rev Med Chir Soc Med Nat Iasi. 112(2): 432-6.
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