Concanavalin A (Con A) Agarose

Concanavalin A (Con A) Agarose consists of Con A coupled to agarose by the Sodium Metaperiodate 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: 6% agarose

Applications

• Purification/ enrichment of of glycoproteins, polysaccharides and glycolipids