|Unit Size||2 ml|
|Country of Manufacture||United States|
|Applications||Glycobiology, Affinity Chromatography|
|Sugar Specificity||Mannose, Glucose|
Pisum sativum agglutinin is nearly identical in structure and carbohydrate specificity to Lens culinaris agglutinin. The lectin has specificity toward α-linked mannose-containing oligosaccharides, with an N-acetylchitobiose-linked α-fucose residue included in the receptor sequence. Calcium and manganese ions are required for activity. PSA has been used to fractionate cells, to isolate glycoproteins and glycopeptides, to distinguish between normal and virally transformed cells, as a T-cell mitogen, and as an inhibitor of allograft rejection.
Agarose bound* Pisum sativum agglutinin is prepared using our affinity-purified lectins. Heat stable, cross-linked 4% agarose beads with a molecular weight exclusion limit of about 2x107 daltons are used as the solid-phase matrix to which the lectins are covalently coupled. The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions. The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix. This coupling method provides several advantages over the traditional cyanogen bromide procedure:
Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads. The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads. Each lot is tested for its binding capacity using glycoproteins known to bind the lectin. This provides a guideline for the user and assures the quality of our agarose bound lectins.
Inhibiting/Eluting Sugar: mixture of 200 mM α-methylmannoside/200 mM α-methylglucoside
*3 mg lectin/ml gel