E-Cadherin is a single-pass transmembrane protein that consists of five extracellular cadherin (EC) domains, a transmembrane domain, and a cytoplasmic tail. The extracellular domains are responsible for homophilic interactions, meaning E-Cadherin molecules on adjacent cells bind to each other, facilitating cell-cell adhesion. These interactions are calcium-dependent, requiring calcium ions to maintain the structural integrity of the cadherin-cadherin binding.
The cytoplasmic tail of E-Cadherin interacts with catenins, which link the cadherin to the actin cytoskeleton. This connection is essential for the stability and function of adherens junctions, which are specialized structures that mediate strong cell-cell adhesion in epithelial tissues.
E-Cadherin is vital for the development and maintenance of epithelial tissues. It regulates various cellular processes, including cell polarity, differentiation, and migration. Loss or dysfunction of E-Cadherin is associated with several pathological conditions, particularly cancer. Reduced expression or function of E-Cadherin can lead to increased cell motility and invasiveness, contributing to tumor progression and metastasis.
Recombinant human E-Cadherin is produced using genetic engineering techniques, where the E-Cadherin gene is inserted into a suitable expression system, such as human embryonic kidney (HEK293) cells. The recombinant protein is then purified and characterized for various applications in research and biotechnology.
Key Characteristics of Recombinant Human E-Cadherin:
Recombinant human E-Cadherin is widely used in research to study cell adhesion, signal transduction, and cancer biology. It serves as a valuable tool for investigating the molecular mechanisms underlying epithelial cell behavior and the role of E-Cadherin in disease processes.