Lectin from Triticum vulgaris

MFCD00147408

NA.56

lyophilized

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.

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.

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.

Molecular characteristics and specificity for sugar binding

≥55% (GE)

powder

agglutination assay: suitable using fresh human erythrocytes

2-8℃

13 - Non Combustible Solids

WGK 3

Eyeshields, Gloves, type N95 (US)