Agilent, GKE-5006A-05, AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/mL

AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/mL. Enzyme (a recombinant form of PNGase F) releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Supplied as 5 vials of GKE-5006A (5 x 100 mU, ≥2.5 U/mL, 1 mM EDTA). Includes 5x N-glycanase reaction buffer, denaturation solution, detergent solution, 5x N-glycanase Tris reaction buffer (MS applications). For a more concentrated formulation of ≥ 10 U/mL, which may be useful for native digestions, see GKE-5010B or GKE-5020B (EDTA-free).

Specifications:
Concentration: ≥2.5 U/mL
Enzyme Applications: Preparation of deglycosylated proteins for molecular weight estimation or crystallography studiesRelease of intact N-linked glycans from glycopeptides and glycoproteinsStructure-function studies of N-glycosylated glycoproteins
Enzyme Formulation: 20 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA (pH 7.5)
Enzyme Source: Recombinant gene from Elizabethkingia meningoseptica, expressed in E. coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum [1]. Enzyme is also known asPNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
Enzyme Specificity: Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless α(1-3) core fucosylated, as in plant glycans and some insect glycans. Asparagine must be peptide bonded at both termini. Phosphate, sulfate, and sialic acid groups attached to the oligosaccharide do not affect cleavage. This product is Endo F free.
Enzyme Unit Definition: One unit is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 μmole of denatured ribonuclease B per minute at 37°C, pH 7.5.
Molecular Weight: ~35,000 daltons
Unit: 500 mU
Volume: 40 µL
pH Optimum: 8.6
pH Range: 7.5-9.5

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AdvanceBio N-Glycanase is a highly purified recombinant Peptide N-Glycosidase F enzyme formulated at a concentration of 2.5 Units per mL. It is specifically designed for efficient cleavage and release of N-linked oligosaccharides from glycoproteins under denaturing or non-denaturing conditions. This enzyme enables rapid and reliable deglycosylation, which is essential for structural characterization, glycan profiling, and quality control in biopharmaceutical development and research.

Ideally suited for use in biopharma and academic laboratories, this solution can be seamlessly integrated into workflows involving the preparation of samples for liquid chromatography or mass spectrometry analysis. AdvanceBio N-Glycanase facilitates high-yield glycan release across various sample types, while maintaining protein backbone integrity.

It is fully compatible with Agilent’s AdvanceBio Glycan Mapping kits, UHPLC columns, and sample preparation tools, supporting streamlined glycoprotein analysis. The enzyme can be utilized with automated systems for high-throughput applications as well as in manual bench-top protocols. AdvanceBio N-Glycanase supports research applications such as glycoprotein characterization, antibody glycosylation analysis, and quality control of therapeutic proteins, enabling detailed glycan structure elucidation and consistent analytical results.