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.
Horseradish peroxidase (HRP) is a 40 kDa protein that catalyzes the oxidation of substrates by hydrogen peroxide, resulting in a colored or fluorescent product or release of light as a byproduct of the reaction. It is most commonly used for blotting, immunoassays and immunohistochemistry methods. Agaricus bisporus Lectin (ABA/ABL) is conjugated to HRP at an appropriate ratio to provide optimal staining characteristics.