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E2153

E-Cadherin/Fc Chimera from mouse

>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Synonym(s):

L-CAM, Arc-1, Cell-CAM120/80, Epithelial cadherin, Uvomorulin

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
MFCD03456676
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
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biological source

mouse

Quality Level

100

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

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E-Cadherin/Fc Chimera from mouse >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

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E-Cadherin/Fc Chimera from mouse

Ephrin-A1/Fc Chimera from mouse >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

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E9902

Ephrin-A1/Fc Chimera from mouse

Noggin/Fc Chimera from mouse >95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Sigma-Aldrich

N6784

Noggin/Fc Chimera from mouse

EphB2/Fc Chimera from mouse >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Sigma-Aldrich

E9402

EphB2/Fc Chimera from mouse

biological source

mouse

biological source

mouse

biological source

mouse

biological source

mouse

assay

>90% (SDS-PAGE)

assay

>90% (SDS-PAGE)

assay

>95% (SDS-PAGE)

assay

>90% (SDS-PAGE)

technique(s)

cell culture | mammalian: suitable

technique(s)

-

technique(s)

-

technique(s)

ligand binding assay: suitable

recombinant

expressed in NSO cells

recombinant

expressed in NSO cells

recombinant

expressed in NSO cells

recombinant

expressed in NSO cells

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

monomer calculated mol wt 88.2 kDa, ~120 kDa by SDS-PAGE (reducing)

mol wt

monomer calculated mol wt 46.8 kDa, 50-55 kDa by SDS-PAGE (reducing)

mol wt

55-60 kDa by SDS-PAGE (reducing), calculated mol wt 50 kDa

mol wt

monomer calculated mol wt 85.3 kDa, 100-110 kDa by SDS-PAGE (reducing)

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.[1] 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.[2]
Extracellular domain of mouse E-Cadherin (amino acids 1-709) fused to the carboxy-terminal 6X histidine tagged Fc region of human IgG1.

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.[1] 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.[3] 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.[4]

Physical form

Lyophilized from 0.2 μm filtered solution in 20mM MES, 300mM NaCl, 1mM CaCl2.

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
MKCR6171
MKCH4686
SLBD6496V
071M1378V
079K1556

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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)
Ying Li et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(41), 16462-16467 (2013-09-27)
Epithelial cadherin (E-cadherin), a member of the classical cadherin family, mediates calcium-dependent homophilic cell-cell adhesion. Crystal structures of classical cadherins reveal an adhesive dimer interface featuring reciprocal exchange of N-terminal β-strands between two protomers. Previous work has identified a putative
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
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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Data Sheet - E2153

Instructions

Global Trade Item Number

SKUGTIN
E2153-50UG04061833602478

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