Maackia Amurensis Lectin II (MAL II), Biotinylated

While the specificity of this lectin is unclear, MAL II appears to bind only to specific carbohydrate structures containing sialic acid. Unlike the Sambucus nigra lectin (SNA), which appears to prefer the (alpha-2,6) binding structure of sialic acid, MAL II appears to bind sialic acid with (alpha-2,3) bonds. The tissue staining patterns of MAL I, SNA and MAL II are also very different. Biotinylated black Maha lectin II has the appropriate amount of biotin binding, providing the best staining properties for this lectin. This conjugate contains essentially no unconjugated biotin and is preserved with sodium azide.