Agilent, GKE-5003, PNGase F, Chryseobacterium, native

PNGase F, Chryseobacterium, native. Native PNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. Releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Also available as a recombinant product, AdvanceBio N-glycanse, see GKE-5006A. Includes 5x reaction buffer, denaturation solution, detergent solution.

Specifications:
Application: Structural analysis of O-glycan
Concentration: ≥2 U/mL
Enzyme Applications: PNGaseF is used to release intact N-linked glycans from glycopeptides and glycoproteinspreparation of deglycosylated proteins for molecular weight estimation or crystallography studiesstructure-function studies of N-glycosylated glycoproteins
Enzyme Formulation: 52 mM Tris-HCl, 36 mM NaCl, 9 mM sodium acetate, 5 mM EDTA, 0.02% sodium azide (pH 7.5), glycerol-free formulation
Enzyme Source: Native, purified from Elizabethkingia meningoseptica. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum
Enzyme Specificity: PNGase F releases intact N-linked oligosaccharides from glycoproteins and glycopeptides. The enzyme will not cleave oligosaccharides from a single asparagine residue and cleavage does not occur if there is core α1-3 linked fucose as commonly encountered in plant glycoproteins Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage.
Enzyme Unit Definition: One unit of N-Glycanase 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: 100 mU
Volume: 50 µL
pH Optimum: 7.5

**********The following product description is generated by AI and is for reference only. If you have any questions, please contact customer service.**********
This native enzyme, derived from Chryseobacterium species, efficiently cleaves N-linked oligosaccharides from glycoproteins, making it indispensable for detailed glycan analysis in biopharmaceutical and academic research. The product enables the complete deglycosylation of various glycoproteins without requiring denaturing conditions, preserving protein structure and activity for sensitive applications.

Ideal for mapping and profiling N-glycosylation sites, this enzyme streamlines workflows in glycoproteomics, biosimilar development, and quality control testing. Its broad substrate specificity accommodates a wide range of glycoprotein types, including antibodies, hormones, and cell surface proteins.

Designed for seamless integration with leading analytical platforms, such as Agilent HPLC, LC-MS, and CE systems, it ensures robust and reproducible results. The enzyme is also compatible with related glycomics sample preparation kits and labeling chemistries, enhancing flexibility across diverse experimental setups.

Each lot is stringently tested for activity and purity, ensuring consistency and reliability vital for both high-throughput screening and intricate structural glycan studies. With this reagent, researchers can achieve precise characterization of glycosylation patterns, supporting advancements in therapeutic protein development and diagnostic biomarker discovery.