Biotinylated Sophora Japonica Agglutinin (SJA)

Sophora japonica agglutinin consists of two subunits, each of which is composed of two chains dissociable by disulfide reducing agents.



SJA has a specificity toward carbohydrate structures terminating in N-acetylgalactosamine and galactose residues, with preferential binding to β anomers. Binding activity of SJA seems to be enhanced at alkaline pH values.



Biotinylated Sophora japonica agglutinin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium sodium azide.



This biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System. First the biotinylated lectin is added, followed by the VECTASTAIN^® ABC Reagent, Avidin D conjugate, or streptavidin derivative.







Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine