Glycine max agglutinin (SBA) is isolated is purified by affinity chromatography. It is consists of four subunits of identical size. SBA has specificity for blood groups A1, A2, and B, and interacts better with neuramidase-treated cells than untreated cells. This lectin has selective affinity for lymphocytes and human CD34+ hematopoietic stem cells. Immobilized conjugates of SBA are important tools for removing T-cells in bone marrow transplants.
Cy5, when bound to Glycine max (Soybean) Lectin (SBA), 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.