Affinity purified Hippeastrum hybrid lectin (HHL) is consists of four subunits of identical size. It binds only to (Î±-1,3) and (Î±-1,6) linked mannosyl units of Î±-mannose residues. HHL reacts not only with terminal but also with internal Î±-D-mannosyl residues. Lectin appears to possess extended binding sites complementary to at least three 1,6-linked Î±-mannosyl. HHL also binds to some yeast galactomannans. 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 Hippeastrum hybrid Lectin (HHL) 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.