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Merck

EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

Synonym(e):

N-Glycosidase F, PNGase F, Peptide N-glycosidase

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About This Item

UNSPSC-Code:
41131616
Preise und Verfügbarkeit sind derzeit nicht verfügbar.

Rekombinant

expressed in E. coli

Qualitätsniveau

Konjugat

(N-linked)

Qualität

Proteomics Grade

Form

ready-to-use solution

Versandbedingung

wet ice

Lagertemp.

2-8°C

Allgemeine Beschreibung

Peptide-N-glycosidase F (PNGase F) belongs to an enzyme family, that are mainly used for the deglycosylation of N-linked glycans.[1]

Anwendung

PNGase Fast may be used to immobilize in order to perform deglycosylation.[1] It may also be used to immobilize onto methacrylate based monolithic support to release the N-linked carbohydrate moieties from glycoproteins.[2]

Biochem./physiol. Wirkung

Peptide-N-glycosidase F (PNGase F) cleaves asparagine-linked high mannose,[3] hybrid and complex oligosaccharides from glycoproteins. It can also deaminate the asparagine to aspartic acid.[4] 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.

Lagerklassenschlüssel

10 - Combustible liquids


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Jana Krenkova et al.
Journal of chromatography. A, 1216(15), 3252-3259 (2009-03-10)
A reactor with immobilized peptide-N-glycosidase F on a monolithic polymer support in a capillary has been developed that allows fast and efficient release of N-linked glycans from immunoglobulin G molecules. Two different monolithic scaffolds based on poly(glycidyl methacrylate-co-ethylene dimethacrylate) and
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
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)
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

Artikel

Fast assessment of antibody-dependent cell-mediated cytotoxicity (ADCC) and glycoform pattern of a therapeutic antibody rituximab by FcγRIIIa affinity chromatography.

Find deglycosylation kits for your research. Review the different features of deglycosylation kits for glycoproteins, enzymatic proteins, and native proteins.

PNGase Fast denaturing buffer and enzyme provide results similar to a conventional 20-hour protocol, reducing workflow time to about 1 hour.

This application note describes the released N-Glycan analysis of a monoclonal antibody, cetuximab, labeled with procainamide, using a BIOshell™ Glycan HPLC column.

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