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.
Cy5, when bound to Maackia amurensis Lectin (MAA/MAL I), can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlap with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens.