Con A-μSphere 4B

Con A-μSphere 4B with immobilized Concanavalin A is an affinity chromatography media for capture of glycosylated biomolecules including glycoproteins and glycolipids. Stronger affinity for α-D-glucose than α-D-mannose

• Concanavalin A (Con A) binds molecules that contain α-D-mannose, α-D-glucose, and sterically related residues with available C-3, C-4, or C-5 hydroxyl groups
• Group-specific adsorbent for molecules containing sugars.
• Highly suitable for isolation of cell surface glycoproteins from detergent-solubilized membranes
• Concanavalin A (Con A) binds molecules that contain α-D-mannose, α-D-glucose and sterically related residues with available C-3, C-4, or C-5 hydroxyl groups
• Highly suitable for isolation of cell surface glycoproteins from detergent-solubilized membranes
• Con A coupled to Sepharose 4B via cyanogen bromide activation

Con A Sepharose is Concanavalin A coupled to Sepharose 4B by the cyanogen bromide method. Concanavalin A (Con A) is a tetrameric metalloprotein isolated from Canavalia ensiformis (jack bean). Con A binds molcules containing α-D-mannopyranosyl, α-D-glucopyranosyl and sterically related residues. The binding sugar requires the presence of C-3, C-4 and C-5 hydroxyl groups for reaction with Con A. Con A coupled to Sepharose is routinely used for separation and purification of glycoproteins, polysaccharides and glycolipids.