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isolated from Sophora japonica (Japanese pagoda tree) seeds
Sophora japonica agglutinin is a glycoprotein with an isoelectric point of about pH 5.5 and consists of two subunits of approximately 60,000 daltons each. Each subunit is composed of two chains of about 30,000 daltons, dissociable by sulfhydryl reducing agents.
SJA has a specificity toward carbohydrate structures terminating in N-acetylgalactosamine and galactose residues, with preferential binding to b anomers. Binding activity of SJA seems to be enhanced at alkaline pH values.
Inhibiting/Eluting Sugar: 200 mM N-acetylgalactosamine |