Galanthus Nivalis Lectin (GNL), Biotinylated

Unlike most mannose-specific lectins, Galanthus nivalis is not a metal protein and does not require ca2 + or N ++ binding. Binding appears to be directed preferentially towards structures containing (alpha-1,3) mannose residues. Unlike most mannose-binding lectins, GNL does not bind alpha-linked glucose. Reports suggest that this lectin binds IgM in rats and mice, but not IgG. The only protein reported to bind to this lectin in human serum is α2-macroglobulin. GNL binds to many viral glycoproteins. The biotinylated cabbage flower lectin binds the appropriate amount of biotin to provide the best staining properties for this lectin. This conjugate contains essentially no unconjugated biotin and is preserved with sodium azide.