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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 <0.1µg/mL following trypsin treatment of the cells. Adding 300mM 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.
Agglutination activity is expressed in μg/mL and is determined from serial dilutions in phosphate buffered saline, pH6.8, of a 1mg/mL solution. This activity is the lowest concentration to agglutinate a 2% suspension of human erythrocytes after 1 hour incubation at 25°C.
application:Suitable for use in ELISA.
Sicherheits Hinweise / Safety
Klassifizierungen / Classificationeclass-Nr: 34-16-04-90
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