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Technical Data Sheet

CM1681

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E-Cadherin (Cytoplasmic)
Mouse Monoclonal IgG1
Price
Size
Species Reactivity
MW

$245
100 μl
Hu, Rt, Ms
120 kDa

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Enlarge

Western blot image of human A431 cells treated with pervanadate (1 mM) for 30 min (lanes 1 & 3) then treated with akaline phosphatase (lanes 2 & 4). Blots were probed with anti-E-Cadherin (Cytoplasmic) and anti-N-Cadherin (Tyr-860)/E-Cadherin (Tyr-835) conserved site.

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Enlarge

Formalin fixed, citric acid treated parafin sections of embryonic Rat E16 intestines. Sections were probed with anti-E-Cadherin (CM1681) then anti-mouse:HRP before detection using DAB. (Images provided by Carl Hobbs and Dr. Pat Doherty at Wolfson Centre for Age-Related Diseases, King's College London).

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Application
Dilution


ELISA
1:2000


ICC
1:250


IHC
1:50


IP
1:100


WB
1:1000



End user should determine optimal dilution for their particular applications and experiments.Western blot membranes were incubated with diluted antibody in 5% non-fat milk, PBS, 0.04% Tween20 for 1hour at room temperature.
Product References
Milara, J. et al. (2013) Thorax. 68(5):410-20. IF: human pulmonary tissue
Vittal, R. et al. (2013) AJP Lung Cell Mol Phys 304(6):401. WB: Rat & Human Epithelial Cells
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Background
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 can disrupt cadherin binding to β-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.


Background References
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.
Immunogen
Clone (M168) was generated from a mouse recombinant E-Cadherin protein containing amino acids in the C-terminal region. This sequence is highly conserved in human and rat E-cadherin.
Buffer and Storage
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Specificity
This E-cadherin antibody detects a 120 kDa* protein in human A431 cells, and does not cross-react with VE-cadherin or N-cadherin.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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