Allium sativum Lectin (ASA) - Pure
Allium sativum lectin (ASA) is isolated from garlic bulbs and purified by affinity chromatography, followed by gel filtration. It is a dimer of two subunits with a molecular weight of 24,000 with an isoelectric point that ranges between pH 7.2 and pH 7.4.
This lectin`s sugar specificities can be elucidated by hemagglutination inhibition and a coupled enzyme-based assay. The hemagglutination inhibition study helps confirm this lectins specificity for D-mannose, while a sensitive enzyme-based assay can examine detailed binding specificities. Binding sites of ASA accommodate a number of ?1-2-linked mannose residues, with an eluting sugar of mannose. Interaction with glycoproteins not only suggests that the lectin recognizes internal mannose but that also binds to the core pentasaccharide of N-linked glycans even when it is sialylated. Although the binding site can withstand terminal sialic acids and the penultimate galactose residues, the removal of sialic acids enhances potency.
This product comes in lyophilized form and is stored below -20ºC.
|Molecular Weight||:||48 kDa|
|Appearance Form||:||White to off-white|
|Shelf Life||:||2 years|