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 GalÎ²1->4GlcNAc as the core binding site with additional one to four sugar subsites and is most complementary to a linear trisaccharide. Some GalÎ²1-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. Affinity purified Erythrina cristagalli (Coral tree) Lectin (ECL/ECA) is immobilized on aminated paramagnetic beads using EDC and stabilized in a buffer to retain maximum activity. These beads are ideal for iP applications to pull down glycoproteins.