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.
Alkaline phosphatase (AP) is conjugated to Glycine max (Soybean) Lectin (SBA) to show the binding of SBA in many applications including Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups from a substrate resulting in a colored or fluorescent product. The optimal enzymatic activity of this protein is between pH 8 and 10, and its reaction rate remains linear, improving sensitivity over time.