Triticum vulgaris Lectin (WGA) - Polystyrene Beads

Wheat Germ Agglutinin (WGA)-Coupled Polystyrene Beads

Wheat germ lectin isolated from Triticum vulgaris is a 36 kDa protein/glycoprotein consisting of two identical subunits. WGA contains a group of closely related isolectins, with an isoelectric point about pH 9. The receptor sugar for WGA is N-acetylglucosamine. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues. This lectin has proven useful for the purification of insulin receptors and for neuronal tracing studies. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans and glycolipids can also bind WGA. Other applications include blood grouping and erythrocyte polyagglutination studies, mitogenic stimulation of lymphocytes and fractionation of cells and other particles.

bioWorld’s Wheat Germ Lectin (WGA) coupled polystyrene beads are supplied as a 5% suspension.

Technical Specifications:

Ligand Source: Triticum vulgaris

Matrix: Polystyrene Beads

Matrix activation: EDC

Matrix attachment: Amide

Ligand density: 1-2 mg Wheat Germ / mL of settled gel

Binding Capacity: 2-3 mg/mL

Inhibiting/Eluting Sugar: Chitin hydrolysate or GlcNAc with acid or salt

Carbohydrate for Elution: 0.2M Chitin hydrolysate or GlcNAc with acid or salt

Blood Group Specificity: A, B, O

Form: 50:50 Liquid Suspension, PBS (1x) pH 7.4 w/ 0.01% Thimerosal

pH stability: 4 - 9

Storage: 2 - 8 C, DO NOT FREEZE

Application note: Calcium is required for binding.

References

• Dale, G.L., and T. Suzuki. 1988 J Cell Biochem. Sep 38 (1): 1-11.

• Stähli, C., M. Caravatti., M. Aeschbacher, C. Kocyba, B. Takacs, and H. Carmann. 1988. Cancer Research 48, 6799-6802