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EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

Synonyme(s) :

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

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About This Item

Code UNSPSC :
41131616

Produit recombinant

expressed in E. coli

Niveau de qualité

200

Conjugué

(N-linked)

Qualité

Proteomics Grade

Forme

ready-to-use solution

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Catégories apparentées

Description générale

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.

Actions biochimiques/physiologiques

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.

Code de la classe de stockage

10 - Combustible liquids

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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
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
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)
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Articles

Correlation of FcR Affinity Chromatography with Glycan Pattern and ADCC Activity of a Therapeutic Antibody

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

Correlation of FcR Affinity Chromatography with Glycan Pattern and ADCC Activity of a Therapeutic Antibody

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

Correlation of FcR Affinity Chromatography with Glycan Pattern and ADCC Activity of a Therapeutic Antibody

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

Correlation of FcR Affinity Chromatography with Glycan Pattern and ADCC Activity of a Therapeutic Antibody

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

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