Erythrina cristagalli lectin or agglutinin (ECL/ECA) is affinity purified lectin consists of two subunits with molecular weights of 28,000 and 26,000. ECL binds to carbohydrate structure in membrane and serum glycoproteins of mammalian cells. The shape of the lectin binding domains may resemble cavity type with Galβ1->4GlcNAc as the core binding site with additional one to four sugar subsites and is most complementary to a linear trisaccharide. Some Galβ1-related oligosaccharides are the major structures for lectin binding. Lectin binding activity can be abolition through salic acid substitution. This allows for specificity to fractionate and isolate mammalian glycoproteins.
Erythrina cristagalli (Coral tree) Lectin (ECL/ECA) is labeled with tetramethylrhodamine isothiocyanate (TRITC) and has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. TRITC is a bright orange or red-fluorescent dye with excitation ideally suited to the 532-nm laser line. TRITC labeled ECL/ECA can be used for cellular imaging applications.