Wheat germ agglutinin (WGA), biotinylated

Wheat germ agglutinin (WGA) contains a group of closely related isolectins, with an isoelectric point about pH 9. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). This lectin is used for the purification of insulin receptors and for neuronal tracing. Biotinylated WGA 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: Chitin Hydrolysate or 500 mM N-acetylglucosamine with salt and/or acid elution generally required

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