Maclura pomifera agglutinin or lectin (MPA/MPL) is tetrameric plant protein purified by fractionation. MPA has a molecular weight of about 44,000 and consists of four subunits. It has an isoelectric point between pH 4.8 and pH 5.3, and blood group specificity towards A, B, and O (-SA). This lectin has a high affinity for tumor-associated T-antigen disaccharide (Galβ1,3GalNAcα) and many O-linked glycopeptide structures. The structure of Galβ1,3GalNAcα occurs on the surface of tumor cells as a mucin-associated antigenic marker, termed as T-antigen. It is also the central element in O-linked glycopeptide structures on other mammalian glycoproteins.
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. Maclura pomifera Lectin (MPL/MPA) is conjugated to HRP at an appropriate ratio to provide optimal staining characteristics.