Triticum vulgaris lectin (WGA)
For Research Use Only
Wheat germ agglutinin (WGA) is isolated from Triticum vulgaris (Wheat germ) by affinity chromatography. It has two subunits and a molecular weight of 36 kDa. The WGA lectin selectively binds to N-Acetyl glucosamine (GlcNAc) and to N-acetylneuraminic acid (sialic acid) residues of glycoproteins and glycolipids.
The lectin agglutinates erythrocytes and most types of malignant cells more readily than the same cells from normal tissues. WGA 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 and Con A are the two lectins most widely used as analytical and preparative agents when studying glycoproteins and cell surface proteins. The immobilized lectins can be used for affinity chromatography of cells and sub-cellular particles.
Triticum vulgaris lectin is supplied as a white to pale-yellow lyophilized powder from 10 mM CH3COONH4. No preservatives are added.For laboratory use only.
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Sugar specificity: N-acetylglucosamine and N-acetylneuraminic acid residues.
Agglutinates erythrocytes and most types of malignant cells.
Agglutinates rabbit erythrocytes at ≤0.1 µg/ml after treating the cells with trypsin.
|Appearance: White to pale yellow lyophilized powder or flocculate. |
Source: Wheat germ.
Molecular weight: 36 kDa.
Sugar specificity: GlcNAc.
Activity: Agglutinates erythrocytes and most types of malignant cells.
Microorganisms: <100 CFU/g.
Protein content: >85%, OD280nm (ε1.6 = 1 mg/ml).
Identity: SDS-PAGE, three bands - the three isolectins.
Shelf life: >Three years when stored at -20°.
|Studies of glycoproteins and glycolipids. |
Purification of membrane proteins.
Affinity chromatography of cells and sub-cellular particles.
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