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PNGase F – Hydrolysis of N-glycans
PNGase F (Peptide N-glycosidase F) is a glycoamidase hydrolyzing the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high-mannose oligosaccharides.
SmartEnzymes™
The enzyme is widely used for sample preparation prior to MS analysis – to reduce the protein heterogeneity and enable released glycan analysis – and to study the functional role of the N-glycan.
Why PNGase F?
- Efficient hydrolysis of all mammalian N-glycans
- Activity on a wide range of glycoproteins
- Available immobilized in ready-to-use spin columns
- Automation-friendly format for high-throughput N-glycan removal
N-linked glycans on glycoproteins
15+ min reaction time
No need for co-factors
Hydrolyzes the glycosidic bond between N-glycans and Asn
Product Formats
PNGase F Immobilized
Immobilized enzyme for hydrolysis of N-glycans on glycoproteins in spin columns
Buy productPNGase F Automation
Lyophilized enzyme in 96-well plates for automated hydrolysis of N-glycans on glycoproteins
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About PNGase F
PNGase F is a glycoamidase hydrolyzing the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high mannose oligosaccharides.
During the reaction, the asparagine residue from which the glycan is removed is deamidated to aspartic acid. The released oligosaccharide is left intact and can be used for further analysis. Removal of N-glycans is widely used for sample preparation for MS analysis to reduce the protein heterogeneity and enable released glycan analysis, and to study the functional role of the N-glycan.
The enzyme is expressed in E. coli from a recombinant gene derived from Elizabethkingia meningoseptica.
Applications
Comprehensive N-glycan profiling using released glycan workflow, supporting sensitive detection and monitoring of critical quality attributes.
Complete Fc N-glycan removal under native conditions, enabling simplfied subunit LC-MS analysis of therapeutic antibodies.
Citations
Resources
SmartEnzymes™ for Automated and High-throughput Characterization of Antibodies
Download Scientific Poster
SmartEnzymes™ for the Glycosylation Charcterization of Glycoproteins
Download Scientific Poster
GlyCLICK® for Generation and Analysis of ADCs
Download Scientific Poster
PNGase F for Improved DAR Determination in Randomly Conjugated ADCs
Download Scientific Poster
FAQ and Support
Is it possible to purchase PNGaseF Immobilized in bulk?
Yes! Contact us at info@genovis.com
Which buffers can be used with the PNGaseF Immobilized column?
The recommended buffer for best performance of the column is TBS buffer at pH 8.6. Other buffers with neutral pH containing 0.15 M NaCl can also be used but optimization may then be required.
Is it possible the reuse the PNGAse F Immobilized column?
No, it is not recommended. We can only guarantee optimal performance for one-time use.
Does PNGase F Immobilized remove all N-linked glycans?
PNGase F Immobilized hydrolyzes the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high mannose oligosaccharides. It does not remove N-glycans with α1-3 core fucosylation.
Can the deglycosylation on the column be performed under denaturing conditions?
The columns are recommended to be used for deglycosylation at native conditions only.
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