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Merck
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EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

동의어(들):

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

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1 KIT
₩717,605

₩717,605

구입 가능 여부는 고객센터에 문의하십시오.
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1 KIT
₩717,605

About This Item

UNSPSC 코드:
41131616

₩717,605

구입 가능 여부는 고객센터에 문의하십시오.

재조합

expressed in E. coli

Quality Level

200

결합

(N-linked)

Grade

Proteomics Grade

양식

ready-to-use solution

배송 상태

wet ice

저장 온도

2-8°C

관련 카테고리

일반 설명

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

애플리케이션

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]

생화학적/생리학적 작용

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.

Storage Class Code

10 - Combustible liquids

가장 최신 버전 중 하나를 선택하세요:

시험 성적서(COA)

Lot/Batch Number
SLBV7894

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COA 검색

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

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
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
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