Wheat germ lectin (WGA) is an affinity-purified lectin that binds to non-enzymes of n-acetyl-D-glucosamine and sialic acid residues of glycoproteins and glycolipids. This lectin protects common wheat from insects, yeast and bacteria. WGA consists of two subunits with a molecular weight of 36,000. It is an acidic protein with mitotic activity on lymphocytes. It can agglutinate red blood cells and most malignant cells. Similar to insulin, WGA can increase the rate of glucose oxidation in isolated fat cells. It inhibits C5a receptor interactions and is used to isolate and isolate insulin receptors. Affinity purified wheat agglutinin (WGA) is coated with microplates and fixed on microplates for enzyme-linked immunosorbent assay. Unoccupied charged groups are blocked by BSA to reduce non-specific interactions and reduce background.
For research use only, not for clinical use.