Merck, 61767-5MG, Lectin from Triticum vulgaris

General description
WGA is not blood group specific but has an affinity for N-acetyl-β-D-glucosaminyl residues and N-acetyl-β-D-glucosamine oligomers. WGA contains no protein-bound carbohydrate.
Lectins are carbohydrate-binding proteins, omnipresent, found in fungi, plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in β-strands and posses a carbohydrate binding sites on the surface.
Application
Wheat germ agglutinin conjugated to the outside surface of PLGA nanoparticles loaded with paclitaxel was used to target cancer cells that overexpress WGA-binding glycoproteins (Caco-2 and HT-29 cell lines). WGA-NP showed 50-60% greater endocytosis and intracellular retention of paclitaxel than unlabeled nanoparticles.
Lectin from Triticum vulgaris has been used in bone resorption assays.
Biochem/physiol Actions
Lectin is known to be useful in glycoconjugate characterizing, imaging and targeting. Its use in a microarray assay, enable efficient glycome profiling. This is because of its specific interaction with oligosaccharides, glycoproteins and glycolipids. In plants and fungi, lectin defends against pathogens/feeders. Lectin participates in host recognition and tissue adhesion, thereby aids in the pathogenesis of microorganism.
Other Notes
Molecular characteristics and specificity for sugar binding