Aleuria aurantia lectin (AaL) (1 gram)
For Research Use Only
Recombinant Aleuria aurantia lectin 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
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.
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Sugar specificity: fucose and terminal fucose residues on complex oligosaccharides and glycoconjugates.
Binding affinity for fucose in all binding positions (α1-2, α1-3, α1-4 and α1-6) Higher affinity towards fucosylated oligosaccharides than native AaL.
Not blood group specific.
Appearance: White to pale yellow lyophilized powder or flocculate.
Molecular weight: Two identical subunits of 36 kDa.
Sugar specificity: Fucose α1-2, α1-3, α1-4 and α1-6.
Activity: Agglutinates human erythrocytes irrespective of blood type (A, B and 0).
Microorganisms: < 100 CFU/g.
Protein content: > 80%.
Identity: SDS-PAGE, 4 mg/ml, staining with coomassie R-350, one band between 30 and 45 kDa.
Shelf life: > Five years when stored at -20°.
Studies of glycoproteins and glycolipids.
Purification of membrane proteins.
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