Overview
E-Cadherin is a classical type I cadherin predominantly expressed in epithelial tissues. As a key component of adherens junctions, it mediates calcium-dependent homophilic cell-cell adhesion through its extracellular domains while linking to the actin cytoskeleton via intracellular catenins. The mouse ortholog (mE-Cadherin) shares ~90% amino acid identity with human CDH1, making it a crucial model for translational research. First identified in the 1980s, E-Cadherin has become a biomarker for epithelial-mesenchymal transition (EMT) in cancer progression. Its downregulation is a hallmark of metastatic invasion, while germline mutations cause hereditary diffuse gastric cancer syndrome. Research-grade mouse E-Cadherin is commonly purified from transfected cell lines or recombinant systems for mechanistic studies.
Physical and Chemical Properties
Mouse E-Cadherin is a 120 kDa single-pass transmembrane glycoprotein with five extracellular cadherin repeats (EC1-EC5), a transmembrane domain, and a highly conserved cytoplasmic tail. The protein requires calcium ions (1-2 mM) for proper folding and adhesive function, with calcium-binding sites located between EC domains. Under non-reducing conditions, it forms stable dimers essential for trans-cellular binding. In solution, purified mE-Cadherin exhibits concentration-dependent aggregation. The extracellular domain (ECD) fragment (≈80 kDa) is often used for structural studies due to higher solubility. The protein is sensitive to proteolysis; working solutions should contain protease inhibitors (e.g., PMSF) and be stored at 4°C for short-term use.
Main Applications
In biomedical research, mouse E-Cadherin reagents are primarily used to: 1) Study epithelial junction dynamics via immunofluorescence or FRET microscopy, 2) Investigate EMT mechanisms in cancer models using knockdown/overexpression systems, and 3) Develop organoid cultures requiring cadherin-mediated self-organization. The extracellular domain is employed in binding assays to quantify homophilic interaction kinetics. Pharmaceutically, E-Cadherin-modulating compounds are explored for metastatic cancer treatment. In toxicology, it serves as a barrier integrity marker for epithelial tissues (e.g., gut, kidney). Recombinant mouse E-Cadherin-Fc chimeras are popular tools for functional studies, offering standardized binding activity and easy detection.
Safety and Storage
While non-hazardous in purified form, E-Cadherin preparations may contain traces of sodium azide (0.02-0.05%) as preservative. Handle with gloves in a biosafety cabinet when reconstituting lyophilized protein. Avoid repeated freeze-thaw cycles; aliquot into single-use portions upon receipt. For long-term storage, maintain at -80°C in neutral buffers (e.g., PBS pH 7.4, HEPES). Lyophilized powder remains stable for 2-3 years at -20°C when desiccated. Working solutions retain activity for 1-2 weeks at 4°C with protease inhibitors. Verify protein integrity by SDS-PAGE if stored beyond 6 months.
B2B Procurement Guide
When sourcing mouse E-Cadherin, prioritize vendors providing: 1) Species-specific validation data (avoid cross-reactive bovine/human contaminants), 2) Functional testing certificates (e.g., cell aggregation inhibition assay), and 3) Detailed buffer composition. For antibody production, request the extracellular domain fragment (ECD) with >95% purity by HPLC. Bulk purchasers (>10 mg) should negotiate batch-to-batch consistency guarantees. Consider recombinant systems (e.g., HEK293, CHO) over tissue-derived protein for better reproducibility. Lead times for custom preparations typically range 4-8 weeks. For cell culture applications, endotoxin levels should be <1 EU/μg.
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