Purified by affinity chromatography, Galanthus nivalis lectin (GNL/GNA) is composed of four identical subunits. GNL is a mannose-binding lectin, though [interestingly] it will not bind α-linked glucose. This lectin was one of the original molecules used to understand how proteins recognize carbohydrates. Galanthus nivalis is found to bind to many viral glycoproteins, making it a useful tool in HIV research studies.
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 Galanthus nivalis Lectin (GNL/GNA) 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.