Sigma-Aldrich E-Cadherin/Fc Chimera from mouse. >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder. 50 μg

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.

E-Cadherin/Fc Chimera from mouse has been used in adhesion assays.[3]

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.[4] 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.[5]

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