A tetramer double chain structure composed of 4 identical propolymers is obtained by affinity chromatography with an isoelectric pH of 7.8. The lectin is specific to blood type O (+SA) and t. Jacalin is considered a galactose-specific lectin that can be eluted with galactose or glycodisaccharide. Jacalin's post-translational proteolytic modification gives lectin a new carbohydrate binding site involving the N end of the α-chain. The structure of this protein explains its carbohydrate binding specificity for the t antigen disaccharide galß 1,3galnac. Effective inhibitors of jacalin include D-galactose, ß-Met-Gal and 2-deoxy-α-d-galactose. Biotin is a small molecule involved in a variety of metabolic processes. This ligand forms complexes with avidin and streptavidin, resulting in the strongest known non-covalent protein-ligand interaction. When using avidin-HRP or streptavidin-HRP couplers, biotinylated AIA has the right amount of biotin binding to provide the best detection characteristics. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications
For research use only, not for clinical use.