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Merck

EMS0001

PNGase Fast

recombinant, expressed in E. coli

동의어(들):

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

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제품정보 (DICE 배송 시 비용 별도)

UNSPSC Code:
41131616
Form:
ready-to-use solution
Recombinant:
expressed in E. coli
기술 서비스
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도움 문의

recombinant

expressed in E. coli

conjugate

(N-linked)

grade

Proteomics Grade

form

ready-to-use solution

shipped in

wet ice

storage temp.

2-8°C

Quality Level

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.

저장 등급

10 - Combustible liquids


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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

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
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
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
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)

문서

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

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

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

Workflows for monoclonal antibody adalimumab characterization ensure drug safety and efficacy through critical quality attribute analysis.

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