Agilent, GKE-5010B-2, AdvanceBio N-Glycanase-plus (PNGase F), ≥10 U/mL

AdvanceBio N-Glycanase-plus (PNGase F), ≥10 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-5010B (5 x 400 mU, ≥10 U/ml, 1mM EDTA). Includes 5x N-glycanase Reaction Buffer:100 mM sodium phosphate pH 7.5, 0.1% sodium azide; denaturation solution: 2% SDS, 1 M 2-mercaptoethanol; detergent solution: 15% detergent; 5x N-glycanase Tris reaction buffer: 50 mM Tris-HCl pH 8.0.

Specifications:
Concentration: 10 U/mL
Enzyme Applications: To obtain efficient deglycosylation of glycoprotein substrates under nondenaturing conditions, it is necessary to use a higher starting concentration of enzyme. N-Glycanase-plus and ULTRA (EDTA-Free) are supplied at ≥ 10 U/ml, and are recommended for all applications requiring deglycosylation of glycoproteins in the absence of denaturants. The high activity also allows smaller reaction volumes and shorter reaction times to be explored.
Enzyme Formulation: 20 mM Tris HCl pH 7.5, containing 1 mM EDTA and 50 mM NaCl
Enzyme Source: Recombinant gene from Elizabethkingia meningoseptica, expressed in E. coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum [1]. Enzyme also known as PNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
Enzyme Specific Activity: ≥10 units/mg
Enzyme Specificity: Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless a(1-3) core fucosylated, as in plant glycans. Asparagine must be peptide bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free. Highly concentrated, particularly useful for deglycosylation under native conditions.
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 pH 7.5 and 37°C.
Unit: 2000 mU
pH Range: 7.5-9.5

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This highly purified recombinant PNGase F enzyme offers efficient and specific removal of N-linked glycans from glycoproteins in research and biopharmaceutical applications. With an activity of at least 10 units per milliliter, the solution ensures reliable and rapid deglycosylation under native or denaturing conditions, accommodating a broad range of sample types including monoclonal antibodies and other therapeutic proteins. The enzyme achieves complete cleavage of N-glycan chains, facilitating detailed glycan profiling and structural analysis via downstream techniques such as HPLC, LC-MS, and capillary electrophoresis.

Designed for seamless integration with Agilent AdvanceBio Glycan Mapping workflows, this reagent supports robust sample preparation prior to chromatographic or mass spectrometric analysis. Its high specificity minimizes non-specific cleavage, reducing sample complexity and streamlining data interpretation. Compatible with a range of glycan labeling chemistries and purification methods, it is ideally suited for laboratories conducting glycoprotein characterization, bioprocess development, biosimilar comparison, and quality control.

Optimized for use with Agilent’s extensive suite of AdvanceBio columns and analytical instruments, as well as related glycan analysis kits, this enzyme delivers consistent performance and reproducible results to support both research and regulated laboratory environments.