Recombinant Human E-Cadherin Protein

Protein Function: E-Cadherin/Cadherin-1, also known as Uvomorulin in the mouse and rat, is a 120 kDa member of the Cadherin family of cell surface glycoproteins that mediate cell adhesion. Human E-Cadherin shares 81% amino acid sequence identity with the rat and mouse proteins. It is a single-pass transmembrane protein that mediates calcium-dependent epithelial cell adhesion. E-Cadherin has five extracellular EC domains that form homophilic cis-clusters between adjacent epithelial cells and trans-clusters within the same cell. E-Cadherin clusters are critical components of adherens junctions between epithelial cells and act in the formation and maintenance of the epithelial cell barrier. The intracellular domain of E-Cadherin binds to the Catenin cytoskeletal complex, which includes p120 Catenin, beta-Catenin, alpha-Catenin, and Vinculin. E-Cadherin expression is critical for epithelial tissue homeostasis. Decreased E-Cadherin is associated with physiological and pathological epithelial-to-mesenchymal transition and cell migration, and E-Cadherin loss contributes to cancer metastasis. The extracellular E-Cadherin N-terminal domain can be cleaved by several proteases and is released as a soluble factor that enhances cancer cell motility and EGFR-dependent survival and proliferation.

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