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 Lectin was conjugated with Biotin, is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction. Biotinylated Agaricus bisporus Lectin (ABA/ABL) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated ABA/ABL allow for more sensitive detection in ELISA and Western-blotting applications. This lectin conjugate is optimized for cellular labeling and detection, making it a valuable tool for enhancing sensitivity in research applications.

Applications: Glycobiology, Immunofluorescence, Immunohistochemistry, Immunocytochemistry

Recommended Usage: Recommended concentrations from 0.5-10 ug/ml in 1XPBS.

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