Vicia villosa lectin (VVL, VVA), Unconjugated

Vicia Villosa Lectin (VVL, VVA), Unconjugated, 5 mg. VVL 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 Vector Laboratories preparations appear to be B subunit–rich. VVL recognizes preferentially alpha- or beta-linked terminal N-acetylgalactosamine, especially a single alpha-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 (alpha-1,3) N-acetylgalactosamine is also a potent inhibitor of this lectin. Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine.