Wheat germ lectin, also known as wheat germ agglutinin (WGA), has a molecular weight of 36 kDa. It shows affinity to 1,4-N-acetylglucosamine (GlcNAc) oligomers and is useful in studying surface components of C. neoformans.
Immunogen
Wheat Germ lectin (WGA)
Application
Anti-Lectin, Triticum vulgaris antibody produced in rabbit has been used in
immunolabeling experiments
immunohistochemistry
immunocytochemistry
Anti-Lectin, Triticum vulgaris antibody produced in rabbit has been used in immunohistochemistry and immunocytochemistry.
Biochem/physiol Actions
Wheat germ agglutinin is a lectin isolated from Triticum vulgaris that has affinity for chitin oligosaccharides, peptidoglycans and glycolipids via sialic acid residues. It is not specific for human blood groups and has been identified as antagonists of botulinum and tetanus toxins.
Target description
Lectins are highly specific carbohydrate binding proteins useful in carbohydrate and cell membrane studies, as well as cell agglutination and typing techniques.
Physical form
Lyophilized from 0.01 M phosphate buffered saline, pH 7.2
Reconstitution
Reconstitute with 2 ml deionized water.
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The Journal of pharmacology and experimental therapeutics, 258(3), 830-836 (1991-09-01)
Lectins from Anguilla anguilla, Artocarpus integrifolia, Canavalia ensiformis, Datora stramonium, Glycine max, Limax flavus, Ricinus communis and Triticum vulgaris were tested for their abilities to antagonize the binding of botulinum neurotoxin and tetanus toxin to rat brain membranes and to
Amygdala projections to the lateral bed nucleus of the stria terminalis in the macaque: comparison with ventral striatal afferents
decamp DM and Fudge JL
The Journal of Comparative Neurology, 521, 3191-3216 (2013)
The binding profile of Triticum vulgaris (WGA, wheat germ) agglutinin to 23 O-glycans (GalNAc alpha1-->Ser/Thr containing glycoproteins, GPs) was quantitated by the precipitin assay and its specific interactions with O-glycans were confirmed by the precipitin inhibition assay. Of the 28
Detection of local and remote cellular damage caused by spinal cord and peripheral nerve injury using a heat shock signaling reporter system
The capsule of Cryptococcus neoformans is a complex structure whose assembly requires intermolecular interactions to connect its components into an organized structure. In this study, we demonstrated that the wheat germ agglutinin (WGA), which binds to sialic acids and beta-1,4-N-acetylglucosamine
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