Glycine max lectin is isolated from soy bean (Soy bean agglutinin, SBA) and purified by affinity chromatography. The molecular weight of the lectin is 120 kDa, it consists of four identical subunits of 30 kDa each and it displays carbohydrate binding specifity for N-acetyl-D-galactosamine and galactopyranosyl residues of glycoproteins. Soybean lectin (Glycine Max) is one of lectins that specifically binds tobeta N-acetyl glucosamine, galactose and mannose sugar residues.

SBA has specificity for blood groups A1, A2 and B. The lectin interacts better with neuramidase-treated cells than with untreated cells. It has selective affinity for lymphocytes and human CD34+ hematopoietic stem cells. Immobilized conjugates of SBA are therefore important tools for removing T-cells in bone marrow transplantation.