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α(1-2,3,6)-Mannosidase. Mannosidase (jack bean) 50 U, ≥150 U/ml, releases nonreducing terminal α(1-2,3,6)-linked mannose from oligosaccharides. Supplied as 5 vials of GKX-5010. Includes incubation buffer [(500 mM sodium acetate, 10 mM zinc chloride (pH 5.0)].

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  • 150 U/mL
Enzyme Formulation
  • 20 mM Tris-HCl, 20 mM NaCl (pH 7.5)
Enzyme Source
  • Jack bean.
Enzyme Specificity
  • The enzyme has broad specificity, cleaving a(1-2,3,6)-linked mannose, although some kinetic preference has been observed (a1-2, 6 > 3). The enzyme will not cleave a single a(1-6) linked mannose residue from core ß-mannose, but will, however, remove a single a1-3 linked mannose from the core ß-mannose. By using enzyme concentrations of around 50 U/ml and extended incubation times (up to 18 hours) at 37°C, complete removal of all nonreducing terminal a-linked mannose residues may be achieved. To expedite glycan sequencing studies, the sluggish activity of GKX-5010 jack bean a mannosidase toward a(1-6)-linked mannose residues can be overcome by using the enzyme in combination with the a mannosidase from Xanthomonas mannihotis that rapidly cleaves a(1-6) linkages. The X. mannihotis a-mannosidase may inhibit the action of other mannosidases if a branched (a1-6) mannose is present in the substrate, so is typically added after incubation of the substrate with jack bean a-mannosidase (GKX-5010).
Enzyme Unit Definition
  • One unit is defined as the amount of enzyme that will hydrolyze 1 µmole of pNP-α-mannopyranoside per minute at pH 4.5 and 37°C.
Molecular Weight
  • ~190 kD
  • 50 U
  • 70 µL
pH Optimum
  • 4.5