Bauhinia purpurea Lectin (BPL/BPA) - AP (Alkaline Phosphatase)

Bauhinia purpurea agglutinin or lectin (BPA/BPL) is a tetrameric lectin with a molecular weight of 120 kDa. Binding appears to be highest for glycoconjugates containing galactosyl (β-1,3) N-acetylgalactosamine structures but oligosaccharides with a terminal α-linked N-acetylgalactosamine can also bind. BPA is lactose-specific and elutes with the sugar lactose. It has specificity for blood groups A, B, O (-SA). Treatment of erythrocytes with neuraminidase or trypsin will increase the agglutination reaction, indicating that the receptor is masked by terminal carbohydrates. Although binding specificity is similar to that of peanut agglutinin, tissue staining patterns of these two lectins are distinct. Alkaline phosphatase (AP) is conjugated to Bauhinia purpurea Lectin (BPL/BPA) to facilitate the visualization of BPL/BPA binding in various applications, including Western blotting and ELISA. Alkaline phosphatase is a large protein with a molecular weight of 140 kDa that catalyzes the hydrol