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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.¹ 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 (α1-2, α1-3, α1-4 and α1-6) 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.²

Recombinant AaL hemagglutinates erythrocytes irrespective of blood type (A, B and 0) at the same titers as AaL isolated from natural sources.

¹ Wimmerova M, Mitchell E, Sanchez JF, Gautier C, Imberty A. Crystal structure of fungal lectin: six-bladed beta-propeller fold and novel fucose recognition mode for Aleuria Aurantia Lectin. J Biol Chem. 2003; 278:27059-67.

² Olausson J, Tibell L, Jonsson BH, Pahlsson P. Detection of a high affinity binding site in recombinant Aleuria Aurantia Lectin. Glycoconj J. 2008; 25:753-62.