After reconstitution with deionized water, the solution may be stored frozen in working aliquots for up to 12 months. The lyophilized powder is stable for more than five years from production date when stored below -20☌. The product is shipped at -20☌ however for over-the-day transport it may be shipped at ambient temperature. In absence of lactose the lectin will polymerize and storage at pH 8.6–8.8 causes precipitation. The solution may be reconstituted in this buffer to desired working concentration. Aggregation is thought to occur in the presence of high concentrations of 2-mercaptoethanol. Spin the vial gently until full dissolution. The lectin may be reconstituted with 2 ml of deionized water before use. Model systems to help understand the molecular basis of how proteins recognize carbohydrates.The lectin is available in vials containing 5 mg powder and is to be used for laboratory work only. The purity of GNA lectin is determined by SDS- electrophoresis, which generates one single band at 13 kDa corresponding to the four identical polypeptide chains. Medicago’s GNA lectin is supplied as a white to cream coloured lyophilized powder. It is also applicable for blood cell agglutination studies but also as a model system to help understand the molecular basis of how proteins recognize carbohydrates. Unlike the majority of mannose-binding lectins, GNA does not bind alpha-linked glucose. It contains little or no carbohydrate and does not need Ca 2+ or Mn 2+ for binding, since unlike most mannose-specific lectins it is not a metalloprotein. Structures containing (α-1,3) mannose residues are preferred for binding (2). It binds specifically to murine IgM immunoglobulin and human α 2-macroglobulin. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes (1). Is has a molecular weight of 50 kDa and consists of four identical subunits (1). Galanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. Binds to serum IgM and α 2- macroglobulin.Sugar specificity: ( α -1,3) mannose residues.

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