Triticum vulgaris (Wheat) lectin (WGA) - Separopore®

Applications:

Wheat germ (Triticum vulgaris) agglutinin (WGA) is a 36,000 molecular weight protein 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. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). WGA-Separopore® 4B-CL has proven useful for the purification of insulin receptors and for neuronal tracing studies. WGA-Separopore® 4B-CL is also used for the purification of glycoproteins containing (D-N-acetylglucosamine)₂ or N-acetylneuraminic acid.

Agarose bound Wheat Germ Agglutinin is prepared from affinity-purified lectin. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2 x 10⁷ are used as the solid-phase matrix to which the lectin is covalently bound. The attachment of the lectin to the solid phase is carefully controlled in order to preserve the activity of the lectin as well as to minimize conformational changes of the bound lectin which might result in nonspecific ionic or hydrophobic interactions.

Technical Specifications:

• Ligand Source: Triticum vulgaris
• Matrix: Separopore® 4B-CL (crosslinked agarose, 4%) 
• Particle size range: 52 – 165 µm
• Matrix activation: Cyanogen bromide
• Matrix attachment: Amino
• Ligand density: 5-10 mg Wheat / mL drained gel
• Binding capacity: 8 mg of N-acetylglucosaminyl glycoprotein/ml drained gel
• Inhibiting/Eluting Sugar: Chitin hydrolysate or GlcNAc with acid or salt
• Carbohydrate for Elution: 500 mM N-acetylglucosamine or 100 mM acetic acid
• Blood Group Specificity: A, B, O

Additional Information

Additional Information

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