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Featuring:
Plus
quality reagents for:
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| Biotinylated Concanavalin A (Con A)
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Con A recognizes α-linked mannose present as part of a “core
oligosaccharide” in many serum and membrane glycoproteins.
At neutral and alkaline pH, Con A exists as a tetramer of
four identical subunits; below pH 5.6, Con A dissociates into
active dimers of 52 kDa. Acetylation, succinylation, or other
derivatizations can also produce stable forms with dimeric
structures. (See succinylated Con A). “Nicks” in the sequence
are often present in the purest preparations due to hydrolytic
damage within the seeds.
Con A requires calcium or manganese ions at each of its four
saccharide binding sites. Although these divalent metal ions
are bound tightly to the polypeptide structure, buffers which
can bind calcium (such as phosphate) generally should be
avoided in diluting Con A, since a gradual loss in activity may
occur.
Biotinylated Concanavalin A 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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