Maackia amurensis Lectin (MAA/MAL I) is a leukoagglutinating lectin isolated from Maackia amurensis seeds and purified by affinity chromatography. MAA I can be used to detect N-linked glycans containing the trisaccharide Siaα2-3Galß1-4GlcNAc. This lectin does not agglutinate one blood type more than another and agglutination can be inhibited by sialyllactose or lactose at higher concentrations. Although MAA I and MAA II are similar in size and structure, this lectin is a more potent mitogen and exhibits less hemagglutinating ability than MAA II.
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 Maackia amurensis Lectin (MAA/MAL I) 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.