Medicago AB Products Are Available Worldwide. For Research Use Only. Recombinant Aleuria Aurantia Lectin (AaL) is produced in E.coli and has an amino acid sequence identical to native AaL. AaL is a dimeric lectin with two identical subunits of approximately 36 kDa. Each subunit has five carbohydrate-binding sites. The lectin recognizes and binds specifically to fucose and terminal fucose residues on complex oligo saccharides and glycoconjugates. rAaL has binding affinity for fucose in all binding positions (alpha1-2, alpha1-3, alpha1-4 and alpha1-6) and in contrast to AaL purified from natural sources, rAaL is not contaminated with free fucose yielding higher affinity towards fucosylated oligosaccharides than native AaL. Recombinant AaL hemagglutinates erythrocytes irrespective of blood type (A, B and 0) at the same titers as AaL isolated from natural sources. AaL has been widely used for analysis and preparation of oligosaccharides and glycoproteins. Diagnostic applications include analysis of disease-associated glycosylation on plasma proteins. Furthermore, rAaL can be immobilized and used for affinity chromatography.