Agaricus bisporus lectin (ABL) isolated from the edible white button mushroom, is composed of two to four very similar isolectins, each a tetramer of approximately 17 kDa subunits. This lectin binds the Thomsen-Friedenreich antigen, also called T disaccharide, galactosyl (β-1,3) N-acetylgalactosamine. Unlike peanut agglutinin, which does not bind sialylated T antigen, ABL binds either sialylated or asialylated forms. Also, whereas peanut agglutinin has a proliferative effect on cancer cells, ABL is anti-proliferative, apparently without cytotoxicity. ABL binds all blood groups and O-linked glycans of IgA subclasses. Simple mono- and disaccharides are only marginally inhibitory.
Biotinylated Agaricus bisporus lectin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.
|Unit Size||1 mg|
|Country of Manufacture||United States|
|Applications||Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Elispot, ELISAs, Glycobiology|
|Sugar Specificity||Gal(b-1,3)GalNAc (T disaccharide)|
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