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. Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Erythrina cristagalli (Coral tree) Lectin (ECL/ECA) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.