Aleuria Aurantia Lectin (AaL) (1 g)
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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 Aleuria Aurantia Lectin. 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.
AaL has been widely used for analysis and preparation of oligosaccharides and glycoproteins.3 Diagnostic applications include analysis of disease-associated glycosylation on plasma proteins.4 Furthermore, rAaL can be immobilized and used for affinity chromatography.5
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.
3 Yazawa S, Kochibe N, Asao T. A simple procedure for isolation of tumor-associated antigens by affinity chromatography using fucose-specific Aleuria Aurantia Lectin. Immunol Invest. 1990; 19:319-27.
4 Hashimoto S, Asao T, Takahashi J, Yagihashi Y, Nishimura T, Saniabadi AR, Poland DC, van Dijk W, Kuwano H, Kochibe N, Yazawa S. alpha1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis. Cancer. 2004; 101:2825-36.
5 Bergström M, Aström E, Påhlsson P, Ohlson S. Elucidating the selectivity of recombinant forms of Aleuria Aurantia Lectin using weak affinity chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 2011 [Epub ahead of print].
Studies of glycoproteins and glycolipids.
Purification of membrane proteins.