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). Furhtermore, rAAL can be immobilized and used for affinity chromatography (5).

運(yùn)輸及保存方法

The product is shipped at -20°C however for over-the-day transport it may be shipped at ambient temperature. The lyophilized powder is stable for more than three years from production date when stored below -20°C. After reconstitution with HEPES buffer, the solution may be stored frozen in working aliquots for up to 12 months.