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

AdvanceBio N-Glycanase-plus (PNGase F), ≥10 U/mL. Enzyme releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. A recombinant form of PNGase F. 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. 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, is 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: 400 mU
Volume: 40 µL
pH Optimum: 8.6
pH Range: 7.5-9.5

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AdvanceBio N-Glycanase-plus (PNGase F) offers efficient and reliable enzymatic release of N-linked glycans from glycoproteins, streamlining workflows in glycan analysis. Supplied at a concentration of at least 10 units per milliliter, this recombinant enzyme rapidly cleaves nearly all types of asparagine-linked complex, hybrid, and high-mannose oligosaccharides. The product is highly suitable for detailed glycoprotein characterization in biopharmaceutical research, including monoclonal antibody analysis, therapeutic protein profiling, and quality control assessments.

Researchers benefit from its compatibility with a variety of sample preparation protocols, both in-gel and in-solution deglycosylation, improving throughput and reproducibility. It integrates seamlessly with Agilent’s comprehensive glycan analysis solutions, such as the AdvanceBio Glycan Mapping columns and 1290 Infinity LC systems. The enzyme’s robust activity also supports downstream applications including HILIC, fluorescence, or mass spectrometry-based glycan detection.

Designed for precision and consistency, this enzyme is ideal for laboratories working on drug development, biosimilar assessment, or glycosylation pattern elucidation. Its user-friendly format helps reduce hands-on time and facilitates high-quality, reproducible data, supporting compliance with regulatory requirements and advancing biological discovery.