Agaricus bisporus agglutinin (ABA) is an affinity-purified tetramer composed of two to four isolectins. ABA has two distinct carbohydrate binding sites, one for galactose-ß-1,3-N-acetylgalactosamine and another for galactose-ß-1,3-N-acetylglucosamine. Agaricus bisporus has an anti-proliferative effect on cancerous cells. ABA can be internalized by clathrin-coated vesicles after binding to surface glycoproteins, thus making ABA an inhibitor of its nuclear import of signal-dependent proteins.
Agaricus bisporus Lectin (ABA/ABL) is labeled with fluorescein isothiocyanate (FITC) and has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. FITC conjugates have been used in a variety of immunohistochemical and flow cytometry applications.