|
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.
This biotinylated lectin conjugate is prepared from affinity-purified lectin and is optimally labeled with biotin. Essentially free of inactive lectin conjugate and containing no free biotin, this biotinylated lectin provides an ideal intermediate for examining glycoconjugates using the Biotin-Avidin System. First the biotin-labeled lectin is added, followed by the VECTASTAIN® ABC Reagent, Avidin D conjugate, or streptavidin derivative. Another possible application is in the isolation of lymphokines and other products of mitogenic stimulation. |