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EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

Sinônimo(s):

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

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About This Item

Código UNSPSC:
41131616
Preço e disponibilidade não estão disponíveis no momento.

recombinante

expressed in E. coli

Nível de qualidade

200

conjugado

(N-linked)

grau

Proteomics Grade

Formulário

ready-to-use solution

Condições de expedição

wet ice

temperatura de armazenamento

2-8°C

Categorias relacionadas

Descrição geral

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

Aplicação

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]

Ações bioquímicas/fisiológicas

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.

Código de classe de armazenamento

10 - Combustible liquids

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Certificados de análise (COA)

Lot/Batch Number
SLBV7894

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

Rapid Glycan Prep & Analysis by LC-MS Workflow

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

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