We offer Sepharose-based affinity chromatography media with immobilized lectin for purification of glycoproteins. Con A Sepharose 4B with concanavalin A (Con A) ligands is useful for isolating mannose and glucose-containing glycoproteins. Lentil Lectin Sepharose 4B also purifies glycoproteins, including detergent-solubilized membrane glycoproteins and viral glycoproteins.
Lectins are proteins that interact specifically and reversibly with certain sugar residues. Their specificity enables binding to polysaccharides and glycoproteins and agglutination of erythrocytes and tumor cells. The interaction between a lectin and a specific sugar residue is analogous to binding between an antibody and an antigen. To select an appropriate lectin-based chromatography media for your purification, it may be necessary to screen different media (resins). Substances bound to the immobilized lectin may be dissociated using a competitive binding substance or an ionic strength gradient.
Immobilized lectins are invaluable tools for isolating and separating glycoproteins, glycolipids, polysaccharides, subcellular particles and cells, and for purifying detergent-solubilized cell membrane components. They also are useful for assessing changes in levels or composition of surface glycoproteins during cell development and in malignant or virally transformed variants.