Pisum sativum agglutinin is nearly identical in structure and
carbohydrate specificity to Lens culinaris agglutinin. The
lectin has specificity toward α-linked mannose-containing
oligosaccharides, with an N-acetylchitobiose-linked α-fucose
residue included in the receptor sequence. Calcium and
manganese ions are required for activity. PSA has been used to
fractionate cells, to isolate glycoproteins and glycopeptides, to
distinguish between normal and virally transformed cells, as a
T-cell mitogen, and as an inhibitor of allograft rejection.
Biotinylated Pisum sativum 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: mixture of 200 mM α-methylmannoside/200
mM α-methylglucoside
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