Triticum vulgaris lectin or Weat germ agglutinin (WGA) is isolated from Triticum vulgaris (Weat germ) and purified by affinity chromatography. The lectin has two subunits and a molecular weight of 36 kDa. WGA selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids. The WGA lectin agglutinates erythrocytes and most types of malignant cells. It agglutinates rabbit erythrocytes at 0.1 μg/ml following trypsin treatment of the cells. Adding 300 mM N-Acetyle-D-Glucosamine gives an inhibition with a titer that is at least 8-fold lower than the control. Wheat germ agglutinin inhibits the C5a receptor interaction, which has implications in studies of receptor micro-heterogeneity and ligand binding sites. WGA together with Con A is the lectin most widely used as an analytical and preparative agent when studying glycoproteins and cell surface proteins. The immobilized lectin can be used for affinity chromatography of cells and sub-cellular particles. WGA is supplied as a white to pale yellow lyophilized powder from a buffer containing 10 mM CH3COONH4. No preservatives are added. The purity of WGA is determined by SDS- electrophoresis which generates three bands, corresponding to the three isolectins of WGA. Protein content is verified in spectrophotmetry.