Vicia villosa lectin (VVL, VVA), biotinylated

This lectin is a family of tetrameric glycoproteins consisting of combinations of A and B subunits similar in structure to PHA and GSL I. The dominant isolectins in our preparations appear to be B subunit-rich. VVL recognizes preferentially α- or β-linked terminal N-acetylgalactosamine, especially a single α-N-acetylgalactosamine residue linked to serine or threonine in a polypeptide (the Tn antigen). Evidence suggests that this lectin also may require specific amino acid sequences at the receptor site of glycosylation. The disaccharide galactosyl (α-1,3) N-acetylgalactosamine is also a potent inhibitor of this lectin. Biotinylated Vicia villosa lectin 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. Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine.

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