Peanut agglutinin (PNA) binds the T-antigen, a galactosyl (β-1,3) N-acetylgalactosamine structure present in many glycoconjugates and other soluble and membrane-associated glycoproteins and glycolipids. With exceptions, the PNA receptor sequence is normally sialylated, which prevents binding to its receptor oligosaccharide (see Jacalin). Sialic acid not bound to receptor sugars may also inhibit binding, and including calcium in diluents can enhance binding. This rhodamine-labeled PNA features a ratio of fluorophores to lectin protein that provides optimal staining (excitation 575 nm, emission 600 nm). It is supplied as a solution essentially free of unconjugated fluorophores.