E2153
E-Cadherin/Fc Chimera from mouse
>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
别名:
L-CAM, Arc-1, Cell-CAM120/80, Epithelial cadherin, Uvomorulin
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关于此项目
Form:
lyophilized powder
Assay:
>90% (SDS-PAGE)
Biological source:
mouse
Recombinant:
expressed in NSO cells
Mol wt:
monomer calculated mol wt 88.2 kDa
~120 kDa by SDS-PAGE (reducing)
calculated mol wt 88.2 kDa
~120 kDa by SDS-PAGE (reducing)
calculated mol wt 88.2 kDa
产品名称
E-Cadherin/Fc Chimera from mouse, >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
biological source
mouse
recombinant
expressed in NSO cells
sterility
sterile; sterile-filtered
assay
>90% (SDS-PAGE)
form
lyophilized powder
mol wt
monomer calculated mol wt 88.2 kDa
~120 kDa by SDS-PAGE (reducing)
calculated mol wt 88.2 kDa
packaging
pkg of 50 μg
technique(s)
cell culture | mammalian: suitable
impurities
endotoxin, tested
UniProt accession no.
shipped in
ambient
storage temp.
−20°C
Quality Level
Gene Information
mouse ... Cdh1(12550)
Application
E-Cadherin/Fc Chimera from mouse has been used in adhesion assays.
Biochem/physiol Actions
E (epithelial)-cadherin is involved in hemophilic cell-cell adhesion in a calcium-dependent manner. It forms adheren junctions through its ectodomains, to maintain physical contacts between adjacent cells. It plays essential roles in developmental processes, tissue homeostasis and multiple diseases. In humans, this protein might be involved in the pathophysiology of ulcerative colitis. In Crohn′s diseased patients, mutations in this gene lead to a truncated or mislocalized protein product. Epithelial-mesenchymal transition (EMT) and mesenchymal-epithelial transition (MET) are the underlying processes of tumorigenesis and embryogenesis, and these involve the control of E-cadherin expression.
General description
E (epithelial)-cadherin is a type I classical cadherin, which exists as a dimer. It has an ectodomain made of five extracellular cadherin-like (EC) domains, connected by conserved linker regions, which are calcium-binding in nature. It spans the membrane once, and contains a cytoplasmic region. It is a glycoprotein, and in humans has a molecular weight of 120kDa. It binds to catenin and cytoskeletal protein with its C-terminal domain.
Extracellular domain of mouse E-Cadherin (amino acids 1-709) fused to the carboxy-terminal 6X histidine tagged Fc region of human IgG1.
Physical form
Lyophilized from 0.2 μm filtered solution in 20mM MES, 300mM NaCl, 1mM CaCl2.
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
Xenopus δ-catenin is essential in early embryogenesis and is functionally linked to cadherins and small GTPases.
Gu D, et al.
Journal of Cell Science, 122(22), 4049-4061 (2009)
Dongmin Gu et al.
Journal of cell science, 122(Pt 22), 4049-4061 (2009-10-22)
Catenins of the p120 subclass display an array of intracellular localizations and functions. Although the genetic knockout of mouse delta-catenin results in mild cognitive dysfunction, we found severe effects of its depletion in Xenopus. delta-catenin in Xenopus is transcribed as
Jessica I Grill et al.
Digestive diseases and sciences, 60(4), 895-902 (2015-01-31)
E-cadherin is a cell adhesion protein with crucial roles in development, tissue homeostasis, and disease. Loss of E-cadherin in the adult intestinal epithelium disrupts tissue architecture and is associated with impaired localization and function of goblet and Paneth cells, reduced
M J Bussemakers et al.
Molecular biology reports, 17(2), 123-128 (1993-02-01)
E-cadherin is a Ca(2+)-dependent cell adhesion molecule involved in cell-cell interaction. In its normal physiological function it plays an important role in embryonic development and tissue morphogenesis. Recent studies have shown that in cancer development E-cadherin can act as a
M Overduin et al.
Science (New York, N.Y.), 267(5196), 386-389 (1995-01-20)
Cadherins are calcium-dependent cell adhesion molecules containing extracellular repeats of approximately 110 amino acids. The three-dimensional structure of the amino-terminal repeat of mouse epithelial cadherin was determined by multidimensional heteronuclear magnetic resonance spectroscopy. The calcium ion was bound by a
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