Wheat germ agglutinin (WGA) contains a group of closely related isolectins that bind N-acetylglucosamine (preferentially the dimers and trimers of this sugar) and oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA also interacts with some glycoproteins via sialic acid residues (see succinylated WGA). This unconjugated WGA is used for the purification of insulin receptors and for neuronal tracing and is supplied as a solution preserved with sodium azide. The recommended inhibiting/eluting sugar is chitin hydrolysate or 500 mM N-acetylglucosamine with salt and/or acid elution.