Concanavalin A (Con A) agarose consists of Con A coupled to 6% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean). It 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. It 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, it is a metalloprotein and to maintain its binding characteristics the presence of both Mn²⁺ and Ca²⁺ is essential. Each subunit of Con A utilises one calcium and one manganese ion and these cations can be removed under acidic conditions abolishing the carbohydrate-binding activity.

Ligand density: 10 to 16 mg Con A/ml resin
Capacity: 20 to 50 mg thyroglobulin/ml resin
Bead structure: 6% agarose
pH stability: 4 to 9