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.
Alkaline phosphatase (AP) is conjugated to Maackia amurensis Lectin (MAA/MAL I) to show the binding of MAA/MAL I in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.