Human E-Cadherin ELISA Kit

Kit Components

 1. Recombinant Human E-Cadherin standard: 2 vials

 2. One 96-well plate precoated with anti- Human E-Cadherin Ab

 3. Sample diluent buffer: 12 mL - 1

 4. Detection antibody: 130 µL, dilution 1:100

 5. Streptavidin-HRP: 130 µL, dilution 1:100

 6. Antibody diluent buffer: 12 mL x1   

 7. Streptavidin-HRP diluent buffer: 12 mL x1

 8. TMB developing agent: 10 mL x1

9. Stop solution: 10 mL x1.

10. Washing solution (20x): 25 mL x1.

Background

Epithelial Cadherin (E-Cadherin), also known as ECAD, Cadherin-1 (CDH1), Cell-CAM120/80, CD324, and Uvomorulin, is a founding member of the cadherin superfamily that plays critical roles in epithelial cell-cell adhesion, morphogenesis, and maintenance of tissue architecture. Mature E-Cadherin is a type I classic transmembrane glycoprotein composed of an extracellular domain with five repeated cadherin domains (C1-C5) and several Ca2+ binding sequences including DAD, LDRE, PENE and DQND located at the interdomain boundaries, a single-pass transmembrane domain and a short C-terminal cytoplasmic domain. In addition to the membrane-bound form, E-Cadherin also occurs in a soluble form (sE-Cadherin), released by the matrix metalloproteases (MMPs) -3 and -7, and plasmin.

Catenin proteins play an important role in regulating E-Cadherin activities. For instance, β- and γ-catenin binds to the catenin-binding domain in the cytoplasmic tail of E-Cadherin. Another catenin, α-catenin, is shown to mediate interactions between the E-Cadherin/β- or γ-catenin complex and the F-actin cytoskeleton directly, or through interactions with several actin-binding proteins including vinculin, afadin, ZO-1, α-actinin, and the zyxin family. Interaction between the E-Cadherin/β-catenin complex and α-catenin is inhibited by the protein IQGAP1, an effector of Rho family members Rac1 and Cdc42. Phosphorylation of β-catenin reduces its binding to E-Cadherin, and thus decreases E-Cadherin adhesive strength.