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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

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NGLYF-RO

N-Glycosidase F

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

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Glycobiology Profiling Tools

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

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PRTR

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FSL

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ISHL Indicated Name

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ISHL Notified Names

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Cartagena Act

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JAN Code

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Certificates of Analysis (COA)

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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)

Identification of N-linked glycosylation sites in human nephrin using mass spectrometry.

Jamshid Khoshnoodi et al.

Journal of mass spectrometry : JMS, 42(3), 370-379 (2007-01-11)

Nephrin is a type-1 transmembrane glycoprotein and the first identified principal component of the glomerular filtration barrier. Ten potential asparagine (N)-linked glycosylation sites have been predicted within the ectodomain of nephrin. However, it is not known which of these potential

Oriented immobilization of peptide-N-glycosidase F on a monolithic support for glycosylation analysis.

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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