Cadherin-1; Cadherin-1; cadherin-1; CAM 120/80; E-Cadherin; uvomorulin; cell-CAM 120/80; OTTHUMP00000174868; epithelial cadherin; cadherin 1, E-cadherin (epithelial); calcium-dependent adhesion protein, epithelial; cadherin 1, type 1, E-cadherin (epithelial); CAM 120/80; Epithelial cadherin; E-cadherin; Uvomorulin
CDH1; CDH1; UVO; CDHE; ECAD; LCAM; Arc-1; CD324; CDHE; UVO
Peptide Sequence: E-Cadherin synthetic peptide corresponds to amino acids in the Cterminal region in human E-cadherin. This sequence is conserved in rat and mouse E-cadherin, and has low homology to other cadherin family members.
The peptide is specifically recognized by anti-E-Cadherin (a.a. 774-786) antibody (CP1921) in ELISA, and has been shown to block the reactivity of CP1921 during Western blot. In addition, the peptide is recommended for use in blocking CP1921 reactivity in immunocytochemistry.
Blocking Peptide is supplied in 50ul phosphate-buffered saline and 0.05% sodium azide.
Store at -20 degree C. Stable for 1 year.
Blocking: 1:1,000. ELISA: 50 ng/well
Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886. Phosphorylation of Tyr-860 (Tyr-835 in E-cadherin) can disrupt cadherin binding to beta-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.
Takeichi, M. (1988) Development 102:639. Xu, Y. et al. (1997) J. Biol. Chem. 272(21):13463. Qi, J. et al. (2006) Mol. Biol. Cell 17(3):1261
NCBI GI登录号 :
Adaptive Immunity Signaling Pathway 366160!!Adherens Junction Pathway 83070!!Adherens Junction Pathway 481!!Adherens Junctions Interactions Pathway 119533!!Apoptosis Pathway 105648!!Apoptotic Cleavage Of Cell Adhesion Proteins Pathway 105680!!Apoptotic Cleavage Of Cellular Proteins Pathway 105678!!Apoptotic Execution Phase Pathway 105677!!Arf6 Trafficking Events Pathway 137954!!Bacterial Invasion Of Epithelial Cells Pathway 149807
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. [provided by RefSeq]
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. Ref.22E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production. Ref.22. 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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.25 Ref.26. 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. Ref.4 Ref.18 Ref.21. Tissue specificity: Non-neural epithelial tissues. Induction: Expression is repressed by MACROD1. Ref.23. Post-translational modification: 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. Ref.4 Ref.12 Ref.15N-glycosylation at Asn-637 is essential for expression, folding and trafficking. Involvement in disease: Defects in CDH1 are the cause of hereditary diffuse gastric cancer (HDGC) [. MIM:137215]. An autosomal dominant 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=Heterozygous germline mutations CDH1 are responsible for familial cases of diffuse gastric cancer. Somatic mutations in the has also been found in patients with sporadic diffuse gastric cancer and lobular breast cancer. Ref.36 Ref.41Defects in CDH1 are a cause of susceptibility to endometrial cancer (ENDMC) [. MIM:608089].Defects in CDH1 are a cause of susceptibility to ovarian cancer (OC) [. MIM:167000]. Ovarian cancer common malignancy originating from ovarian tissue. Although many histologic types of ovarian neoplasms 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. Sequence similarities: Contains 5 cadherin domains. Sequence caution: The sequence AAA61259.1 differs from that shown. Reason: Frameshift at positions 16, 22, 25, 28, 31, 34, 52, 67, 73, 76, 94, 102, 633 and 636.
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