Agilent, GKX-5010, α(1-2,3,6)-Mannosidase (jack bean)

α(1-2,3,6)-Mannosidase (jack bean). Enzyme releases nonreducing terminal α(1-2,3,6)-linked mannose from oligosaccharides. Includes incubation buffer [(500 mM sodium acetate, 10 mM zinc chloride (pH 5.0)].

Specifications:
Concentration: 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 with the a- mannosidase from Xanthomonas mannihotis which 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
Unit: 10 U
Volume: 70 µL
pH Optimum: 4.5

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This highly purified α(1-2,3,6)-mannosidase enzyme, sourced from jack bean, enables efficient and specific cleavage of terminal non-reducing α-linked mannose residues from oligosaccharides, glycoproteins, and glycopeptides. The enzyme’s broad substrate specificity makes it a versatile tool for detailed structural analysis of complex carbohydrates and glycan profiling in biochemistry and molecular biology laboratories. Its use is essential in deglycosylation workflows, characterization of glycoproteins, and elucidating glycan branching patterns, which are critical in biotherapeutic research and quality control.

Suitable for a range of applications, including mass spectrometry-based glycomic studies, HPLC, and capillary electrophoresis, this enzyme can be seamlessly integrated with Agilent’s glycan analysis kits and sample preparation systems. It is also compatible with a wide spectrum of analytical instruments, such as Agilent LC and LC-MS platforms. The product is supplied with detailed usage protocols to optimize reaction conditions and ensure experimental reproducibility. Researchers working in proteomics, glycomics, and biomedical research will find this mannosidase valuable for streamlining the processing and accurate analysis of N-linked glycan structures from diverse biological samples.