Triticum vulgaris (Wheat) Lectin (WGA) – Pure
Wheat germ agglutinin (WGA) is isolated from wheat germ (Triticum vulgaris) and is a protein that reversibly and non-enzymatically binds to N-acetyl-D-glucosamine and sialic acid residues of glycoproteins and glycolipids. This lectin protects Triticum vulgaris from insects, yeast and bacteria. WGA consists of two subunits and has a molecular weight of 36, 000. It is an acidic protein with an isoelectric point greater than pH 9. WGA has mitogenic activity toward lymphocytes. It agglutinates erythrocytes (rabbit erythrocytes at less than 0.1 g/ml following trypsin treatment of the cells) and most types of malignant cells.Studies show that WGA is very effective in enhancing the rate of glucose oxidation in isolated fat cells (maximal effects similar to that achieved with insulin). Studies also report that this lectin inhibits C5a receptor interaction, which has the implications of receptor micro-heterogeneity and ligand binding sites. See other WGA conjugates.This product comes in a lyophilized form and is stable for more than three years when stored below -20° C. Calcium ion is required for binding.