Wheat germ agglutinin (WGA) is affinity purified lectin that 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 and has mitogenic activity toward lymphocytes. It agglutinates erythrocytes and most types of malignant cells. WGA, similar to insulin, enhances the rate of glucose oxidation in isolated fat cells. It inhibits C5a receptor interaction and is used for isolation and fractionation of insulin receptors.
Triticum vulgaris Lectin (WGA) is labeled with fluorescein isothiocyanate (FITC) and has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. FITC conjugates have been used in a variety of immunohistochemical and flow cytometry applications.