EMS0001
PNGase Fast
recombinant, expressed in E. coli
Synonym(s):
N-Glycosidase F, PNGase F, Peptide N-glycosidase
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About This Item
UNSPSC Code:
41131616
Recommended Products
recombinant
expressed in E. coli
Quality Level
conjugate
(N-linked)
grade
Proteomics Grade
form
ready-to-use solution
shipped in
wet ice
storage temp.
2-8°C
Related Categories
General description
Peptide-N-glycosidase F (PNGase F) belongs to an enzyme family, that are mainly used for the deglycosylation of N-linked glycans.
Application
PNGase Fast may be used to immobilize in order to perform deglycosylation. It may also be used to immobilize onto methacrylate based monolithic support to release the N-linked carbohydrate moieties from glycoproteins.
Biochem/physiol Actions
Peptide-N-glycosidase F (PNGase F) cleaves asparagine-linked high mannose, hybrid and complex oligosaccharides from glycoproteins. It can also deaminate the asparagine to aspartic acid. PNGase Fast enables complete and rapid deglycosylation of antibodies and immunoglobulin fusion proteins, as well as other glycoproteins, to be prepared for downstream chromatography or mass spectrometry analysis. PNGase Fast creates an optimized workflow, reducing processing time without compromising sensitivity or reproducibility.
Storage Class Code
10 - Combustible liquids
Certificates of Analysis (COA)
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Customers Also Viewed
David A Fischler et al.
Journal of biomolecular techniques : JBT, 30(4), 58-63 (2019-10-11)
There are several methods, both chemical and enzymatic, to release N-linked glycans for structural characterization. One of the most common enzymatic release methods is the use of peptide:N-glycosidase F (PNGase F). A less expensive and quicker alternative has been reported
N-linked Glycan Release Efficiency: A Quantitative Comparison between NaOCl and PNGase F Release Protocols
Fischler DA and Orlando R
Journal of biomolecular techniques : JBT, 30, 58-58 (2019)
Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis
Krenkova J, et al.
Journal of Chromatography A, 1322, 54-61 (2013)
Multidimensional system enabling deglycosylation of proteins using a capillary reactor with peptide-N-glycosidase F immobilized on a porous polymer monolith and hydrophilic interaction liquid chromatography-mass spectrometry of glycans
Krenkova J, et al.
Journal of Chromatography A, 1216, 3252-3259 (2009)
Jana Krenkova et al.
Journal of chromatography. A, 1322, 54-61 (2013-11-19)
In this paper, we report on a novel oriented peptide-N-glycosidase F (PNGase F) immobilization approach onto methacrylate based monolithic support for rapid, reproducible and efficient release of the N-linked carbohydrate moieties from glycoproteins. The glutathione-S-transferase-fusion PNGase F (PNGase F-GST) was
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