E-Cadherin is composed of an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The extracellular domain mediates homophilic interactions with E-Cadherin molecules on adjacent cells, facilitating cell-cell adhesion . The cytoplasmic domain interacts with catenins, which link E-Cadherin to the actin cytoskeleton, thereby stabilizing cell adhesion and maintaining tissue integrity .
E-Cadherin is essential for the maintenance of epithelial cell layers by regulating cell adhesion, mobility, and proliferation . It plays a pivotal role in embryonic development, tissue morphogenesis, and the maintenance of tissue architecture . Additionally, E-Cadherin functions as a tumor suppressor, and its loss or dysfunction is associated with increased invasiveness and metastasis in various cancers .
Recombinant E-Cadherin (Human) expressed in HEK 293 cells is a valuable tool for research and therapeutic applications. HEK 293 cells are human embryonic kidney cells that are commonly used for the production of recombinant proteins due to their high transfection efficiency and ability to perform post-translational modifications .
The recombinant E-Cadherin protein is typically tagged with a 6-His tag at the C-terminus to facilitate purification and detection . It is lyophilized from a filtered solution in PBS, pH 7.4, and can be reconstituted in sterile PBS for use in various assays .