Aleuria Aurantia Lectin (AaL) (2 mg)
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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.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, Påhlsson P. Detection of a high affinity binding site in recombinant Aleuria Aurantia Lectin. Glycoconj J. 2008; 25:753-62.
Studies of glycoproteins and glycolipids.
Purification of membrane proteins.
Material Safety Data Sheet (MSDS)