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 (1). Rat E-Cadherin shares 92% and 81% amino acid sequence identity with the mouse and human proteins, respectively (2). 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 (3, 4). 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 (5). The extracellular E-Cadherin terminal domain can be cleaved by several proteases and is released as a soluble factor that enhances cancer cell motility and EGF R‑dependent survival and proliferation (6).