Styphnolobium japonicum agglutinin (SJA) is affinity purified from Japanese pagoda tree seeds. It consists of two subunits. The subunits can be separated into two subfractions, a D-galactose/N-acetyl-D-galactosamine specific lectin (B-SJA-I) and a D-mannose/D-glucose specific lectin (B-SJA-II). SJA has an isoelectric point between pH 4.9 and pH 5.6 and a carbohydrate specificity towards Î²GalNAc. This lectin elutes with the sugar GalNAc.SJA agglutinates all blood group types but has greater affinity for A erythrocytes than of B types, than of O (-SA) types. Binding experiments of the lectin with frozen sections of human kidneys shows specific binding to the endothelia in specimens from blood groups B or AB, thus indicating a D-galactose/N-acetyl-D-galactosamine receptor specificity. SJA lacks mitogenic and immune-suppressive activity.Styphnolobium japonicum Lectin (SJA)Â is labeled with tetramethylrhodamine isothiocyanate (TRITC) and has an appropriate number of fluorochromes bound to provide the optimum staining characteristics for this lectin. TRITC is a bright orange or red-fluorescent dye with excitation ideally suited to the 532-nm laser line. TRITC labeled SJAÂ can be used for cellular imaging applications.