Dolichos biflorus agglutinin (DBA) is isolated from horse gram and purified by affinity chromatography. DBA is a glycoprotein with a molecular weight of about 111,000 and consists of 4 subunits of equal size. This lectin has an isoelectric point between pH 4.6 and pH 5.5. It has a carbohydrate specificity toward α-N-acetylgalactosamine and elutes with the sugar GalNAc.
DBA has been used as a general marker of developing renal collecting ducts, which can then be used to establish secretion status in blood group A individuals by hemagglutination inhibition and for detecting blood typing. DBA is over thousand times more active in agglutinating blood group A1 cells versus A2 cells, and is used to distinguish these blood types in routine serology applications, and has potential applications in examining tumors which affect the levels of blood group substances.
Reconstitute with sterile buffer. Calcium, manganese, magnesium, and zinc ions are required for binding.
Cy5, when bound to Dolichos biflorus Lectin (DBA), can show the binding pattern of this lectin in cellular imaging and flow cytometry. The excitation wavelength required for Cy5 to fluoresce is high enough to avoid overlap with most other fluorochromes, making it useful for dual-labeling experiments. Because of this high excitation, there is typically less background from autofluorescence of biological specimens.