Anti-E-Cadherin Antibody

Routinely evaluated by immunoblot with RIPA lysates from HepG2 cells.

Detect E-Cadherin using this Anti-E-Cadherin Antibody validated for use in Immunohistochemistry and WB.

Immunohistochemistry (Paraffin) Analysis: A 1:250 dilution of this antibody detected E-Cadherin in Human small intestine tissue sections.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected E-Cadherin in HepG2 cell lysate.

Research Category
Cell Structure

Research Sub Category
Adhesion (CAMs)

E-Cadherin

Predicted to cross-react with mouse, rat, orangutan, bovine, chicken and canine based on sequence homology

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

106kDa

Cadherin-1 (UniProt: P12830; also known as CAM 120/80, Epithelial cadherin, E-cadherin, Uvomorulin, CD324) is encoded by the CDH1 (also known as CDHE, UVO) gene (Gene ID: 999) in human. Cadherins are calcium-dependent cell adhesion molecules that participate in cell-cell adhesion during embryogenesis, development, organogenesis, and differentiation. E-cadherin is a single-pass type I membrane glycoprotein that is mainly expressed in non-neural epithelial tissues. It is synthesized with a signal peptide (aa 1-22) and a propeptide (aa 23-154) that are subsequently cleaved off to produce the mature form that contains an extracellular domain (aa 155-709), a transmembrane domain (aa 710-730), and a cytoplasmic domain (aa 731-882). N-glycosylation at Asn-637 is shown to be essential for its expression, folding, and trafficking. E-cadherin is known to contain five cadherin domains. 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. Post-translationally it can be cleaved into three chains: E-Cad/CTF1 (aa 701-882); E-Cad/CTF2 (aa 732-882); and E-Cad/CTF3 (aa 751-882). During apoptosis or with calcium influx, it is cleaved by a membrane-bound metalloproteinase (ADAM10; at residues 700-701), which causes disruption of cell-cell adhesion and the subsequent release of b-catenin into the cytoplasm. The residual membrane-tethered cleavage product is then rapidly degraded via an intracellular proteolytic pathway. It can also be cleaved by PS1/g-secretase (at residues 731-732) and this cleavage promotes disassembly of adherens junctions. Caspase 3 can cleave it at residues 750-751, which releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. (Ref.: Marambaud, M., et al. (2002). EMBO J. 21(8); 1948-1956; Steinhausen, U., et al. (2001). J. Biol. Chem. 276(7); 4972-4980; Ito, K., et al. (1999). Oncogene. 18(50); 7080-7090).

synthetic peptide corresponding to amino acids 859-874 of human E-Cadherin

feature_concentration_valuePlease refer to lot specific datasheet.

Serum

2 years at -20°C from date of shipment

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany