Concanavalin A (Con A) Agarose consists of Con A coupled to 4% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean).
Con A is used for the purification of glycoproteins, polysaccharides and glycolipids as it binds molecules containing α-D-mannopyranosyl, α-D-glucopyranosyl and sterically related residues. Con A agarose has also be used in other application areas including purification of enzyme-antibody conjugates, purification of IgM and separation of membrane vesicles.
As stated above, Con A is a metalloprotein and to maintain its binding characteristics the presence of both Mn2+ and Ca2+ is essential. Each subunit of Con A utilizes one calcium and one manganese ion and these cations can be removed under acidic conditions abolishing the carbohydrate-binding activity.
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Features
- Binds α-D-mannopyranosyl, α-D-glucopyranosyl and sterically related residues
- Purification/ enrichment of of glycoproteins, polysaccharides and glycolipids
- Ligand Density: 10-16mg Con A/ml resin
- Capacity: 20-50mg thyroglobulin/ml resin
- Bead structure: 4% agarose
Applications
- Purification/ enrichment of of glycoproteins, polysaccharides and glycolipids