Biotinylated Maackia Amurensis Lectin II (MAL II)

Maackia amurensis lectin II (MAH) is a glycoprotein consisting of two subunits each of which is composed of disulfide-linked chains. Although the specificity of this lectin is not well defined, MAL II appears to bind only particular carbohydrate structures that contain sialic acid. Unlike Sambucus nigra lectin (SNA) which seems to prefer structures with (α-2,6) linked sialic acid, MAL II appears to bind sialic acid in an (α-2,3) linkage. Tissue staining patterns are also very different among MAL I, SNA and MAL II.

Biotinylated Maackia amurensis lectin II has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium sodium azide.

This biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System. First the biotinylated lectin is added, followed by the VECTASTAIN ABC Reagent, Avidin D conjugate, or streptavidin derivative.

Geisler, C and Jarvis, D.L. Glycobiology, vol. 21, no. 8 pp. 988-993, 2011

Inhibitor: Human glycophorin