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.
Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Glycine max (Soybean) Lectin (SBA) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.