Jacalin lectin (AIA) is purified by affinity chromatography and is tetrameric two-chain structure consisting of four identical protomers with an isoelectric point of pH 7.8. The lectin has specificity for blood group types O (+SA) and T. Jacalin is considered a galactose-specific lectin and elutes with galactose or melibiose. A post-translational proteolytic modification of Jacalin gives the lectin a novel carbohydrate-binding site involving the N terminus of the α-chain. The protein’s structure explains it’s carbohydrate-binding specificity of T-antigen disaccharide Galβ1,3GalNAc. Potent inhibitors of jacalin include D-galactose, β-Met-Gal and 2-deoxy-α-D-galactose.
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 Artocarpus integrifolia (Jacalin) Lectin (AIA) 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.