Agaricus bisporus Lectin (ABA/ABL) - Cy5

Agaricus bisporus Lectin (ABA/ABL) is isolated from edible mushroom and purified by using GalNAc Sepharose 4B. This Lectin is composed of four subunits with slightly different amino acid sequences and glycosylation specificity. ABA/ABL Lectin has high affinity for galactose-1,3-N-acetylgalactosamine (Gal-1,3-GalNAc; also known as T-antigen disaccharide) and galactose-1,3-N acetylglucosamine, but does not bind to monosaccharides. ABA is a potent mitogen for T cells and binds to serum protein IgA. 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. Pure BA was conjugated with Cy5, bound to Agaricus bisporus Lectin (ABA/ABL), can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlapping