http://www.creativebiomart.net/description_382891_12.htm

Cadherins are calcium-dependent cell adhesion proteins which preferentially interact with themselves in a homophilic manner in connecting cells, and thus may contribute to the sorting of heterogeneous cell type. E-cadherin (E-Cad), also known as CDH1 and CD324, is the classical cadherin molecule and contains five cadherin domains of ~110 aa each in the extracellular domain. E-Cad is expressed in the non-neural epithelial tissues as disulfide-linked homodimer, and plays a key role in the organization and integrity of most epithelial tissues, cell differentiation and tissue development. CDH1 interacts directly, via the cytoplasmic domain, with CTNNB1 or JUP to form the PSEN1/cadherin/catenin adhesion complex which connects to the actin skeleton through the actin binding of alpha-catenin. During apoptosis or with calcium influx, E-Cad is cleaved by the metalloproteinase to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. E-Cad has been identified as a potent invasive suppressor, as downregulation of E-cadherin expression is involved in dysfunction of the cell-cell adhesion system, and often correlates with strong invasive potential and poor prognosis of human carcinomas (gastric, breast, ovary, endometrium and thyroid).