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10 mg

Ref. BWG-21510856-2

photos non contractuelles

Neuf 518.00 H.T.


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Détails Produit

Product Description
Lectin AAL is isolated from orange peel fungus (Aleuria aurantia). AAL is a diamer of two identical subunits with a molecular weight of 72,000. Each subunit has five carbohydrate-binding sites that recognize and bind specifically to fucose and terminal fucose residues on complex oligosaccharides and glycoconjugates. AAL shows high affinity for Fucα6GlcNAc in the core of N-glycans and gives an elution of 100 mM L-fucose. AAL also reversibly binds fucose attached to nucleic acids. This lectin has an isoelectric point of pH 9 and non-specific blood group.

AAL comes in lyophilized powder form and is stable for more than three years from production date when stored below -20˚C. AAL is available in chromatographically purified, affinity purified and conjugated to various fluorophores, biotin, HRP and immobilized to Separopore (agarose) matrix.

Studies of glycoproteins and glycolipids
Purification of membrane proteins and receptors
Affinity chromatography
Subcellular localization (Histochemistry)
Agglutination studies
ELISA assays


  • Hashimoto S, Asao T, Takahashi J, Yagihashi Y, Nishimura T, Saniabadi AR, Poland DC, van Dijk W, Kuwano H, Kochibe N, Yazawa S. α1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis. Cancer. (2004) 101:2825-36.
  • 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.
  • 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.