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Merck

EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

Sinónimos:

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

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About This Item

Código UNSPSC:
41131616
En este momento no podemos mostrarle ni los precios ni la disponibilidad

recombinante

expressed in E. coli

Nivel de calidad

conjugado

(N-linked)

grado

Proteomics Grade

Formulario

ready-to-use solution

Condiciones de envío

wet ice

temp. de almacenamiento

2-8°C

Categorías relacionadas

Descripción general

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

Aplicación

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]

Acciones bioquímicas o 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 clase de almacenamiento

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
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

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

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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