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.
Texas Red is a red-fluorescent dye and when bound to Triticum vulgaris Lectin (WGA) can show the binding pattern of this lectin in cellular imaging applications. There is very little overlap between the emission spectra of Texas Red and FITC making this combination ideal for dual-labeling experiments. Rhodamine dyes, such as Texas Red, are more photostable and less sensitive to pH change when compared to other dyes such as fluorescein.