GSL II is affinity purified tetramer that contains a single type of 30 kDa subunit. It has insecticidal structure/function, the first GlcNAc binding legume lectin proven to have insecticidal activity.
This lectin has a carbohydrate specificity for αGal and αGalNAc and elutes with galactose or N-acetylgalactosamine. Increasing the number of N-acetylglucosamine residues beyond two does not improve affinity. It has been reported to be unique in its ability to recognize exclusively α- or β-linked N-acetylglucosamine residues on the nonreducing terminal oligosaccharides. This lectin shows specificity for blood group A(-SA) greater than blood group B(-SA).
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 Griffonia simplicifolia Lectin (GSL II) 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.