Bauhinia purpurea agglutinin or lectin (BPA/BPL) was isolated from camel_Ã‘Ã©s foot tree. BPA is a tetrameric lectin with a molecular weight of 195,000 and an isoelectric point between pH 4.6 and pH 6.0. Binding appears to be highest for glycoconjugates containing galactosyl (?-1,3)N-acetylgalactosamine structures but oligosaccharides with a terminal ?-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. Makela`s group 2 sugars, particularly N-acetyl-D-galactosamine, are potent inhibitors. The native protein appears to be stable in detergent solution. This product comes in lyophilized form and is stored at -20Ã«ï¿½C. Reconstitute with sterile buffer. No metal ions are required for binding.