Agilent, GK80050, AdvanceBio β-N-acetylhexosaminidase

AdvanceBio β-N-acetylhexosaminidase. Enzyme cleaves all nonreducing terminal β-linked N-acetylglucosamine (GlcNAc). Also known as N-Acetyl-β-D-glucosaminidase, β-N-Acetylglucosaminidase. β(1-2,3,4,6)-specific. Use with GKX-5003 to determine the linkage position of β-linked GlcNAc residues. Does not release bisecting GlcNAc of N-glycans. No activity toward N-acetylgalactosamine (GalNAc). Includes 5x incubation buffer A [250 mM sodium phosphate pH 5.0].

Specifications:
Concentration: 40 U/mL
Enzyme Applications: Due to the complex nature of the specificity of this enzyme, it has been used extensively for the analysis of the positional isomerism of GlcNAc in glycans. It is complementary to the ß-N-acetylhexosaminidase from jack bean (GKX-5003).
Enzyme Formulation: 20 mM Tris-HCl, 50 mM NaCl (pH 7.5)
Enzyme Source: Recombinant gene from Streptococcus pneumoniae, expressed in E. coli.
Enzyme Specificity: This enzyme releases nonreducing terminal ß(1-2,3,4, and 6)-linked N-acetylglucosamine from complex carbohydrates. When incubated with oligosaccharides at low concentrations (less than 50 mU/ml) the enzyme can differentiate between GlcNAcß1-2Man, GlcNAcß1-4Man and GlcNAcß1-6Man linkages. Under such conditions, the enzyme cleaves only ß1-2 linked GlcNAc, with two provisos. First, ß1-2 GlcNAc is not hydrolyzed if the mannose to which it is substituted has a substitution at C-6. Thus, the enzyme is useful for the analysis of triantennary oligosaccharides. Second, if the ß-linked mannose of the conserved pentasaccharide core is substituted with a 'bisecting' GlcNAc then only the ß1-2 linked GlcNAc linked to mannose on the a1-3 arm is cleaved. At higher concentrations of the enzyme, ß(1-4) and ß(1-6)-linked GlcNAc may also be hydrolyzed. The reported activity against O-linked oligosaccharides suggests that GlcNAc ß1-3Gal and GlcNAc ß1-6Gal are digested1. Although the specificity towards oligosaccharides containing GalNAc is not known, the enzyme, in common with other glucosaminidases, also hydrolyses pNP-ß-GalNAc at pH 6.0 and 37C. The activity towards this substrate is ~7 fold less than towards pNP-ßGlcNAc.
Enzyme Unit Definition: One unit is defined as the amount of enzyme required to catalyze the release of 1 µmole of p-nitrophenol from p-nitrophenol-N-acetyl-ß-D-glucosaminide per minute at 37°C, pH 5.0
Volume: 40 µL
pH Optimum: 5

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AdvanceBio β-N-acetylhexosaminidase is a highly purified recombinant enzyme ideal for precise glycan analysis in biopharmaceutical and academic research workflows. Specially designed for the selective removal of terminal N-acetylglucosamine and N-acetylgalactosamine residues, this enzyme supports comprehensive characterization of N- and O-glycans from diverse biomolecules, including monoclonal antibodies and glycoproteins. Its robust activity ensures efficient deglycosylation under mild reaction conditions, preserving sensitive glycan structures for accurate downstream analysis.

This product is compatible with a wide range of analytical platforms such as Agilent AdvanceBio LC columns, HPLC, and mass spectrometry systems, facilitating seamless integration into established glycoprofiling protocols. Key usage scenarios include bioprocess development, quality control testing, and detailed structural elucidation in glycomics and proteomics research. It is highly recommended for laboratories needing reproducible, high-specificity glycan removal to support regulatory submissions or advanced R&D.

AdvanceBio β-N-acetylhexosaminidase offers reliable performance, batch-to-batch consistency, and is well-suited for both routine and advanced analytical applications. For optimized sample preparation and analytical results, pair with complementary products including Agilent glycan labeling kits and AdvanceBio sample preparation solutions.