Peanut agglutinin (PNA) binds preferentially to the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates such as M and N blood groups, gangliosides, and other soluble and membrane-associated glycoproteins and glycolipids. With some exceptions, the PNA receptor sequence is normally sialylated, which prevents the lectin from binding to its receptor oligosaccharide (see Jacalin). Even sialic acid that is not bound directly to the receptor sugars may inhibit binding. The presence of calcium ions in diluents can enhance the binding of PNA to receptors, possibly by neutralizing the negative charges on sialic acid residues adjacent to the receptor sequence. This conjugate features a ratio of biotin to lectin protein that provides optimal avidin/streptavidin and lectin binding activity. Supplied essentially free of unconjugated biotins, it is preserved with sodium azide.