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.
WGA-HRP can be used for both anterograde and retrograde tracing. Our peroxidase-wheat germ agglutinin is specially prepared for neuronal transport studies. WGA-peroxidase features a high concentration of protein and is supplied in a 2 mg package at 40 mg/ml ready for injection. Unconjugated wheat germ agglutinin, also used in neuronal studies is available as 10 mg and 25 mg of salt-free, lyophilized lectin.
Inhibiting/Eluting Sugar: Chitin Hydrolysate or 500 mM
N-acetylglucosamine with salt and/or acid elution generally required
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