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Merck
CN

EMS0001

Sigma-Aldrich

PNGase Fast

recombinant, expressed in E. coli

别名:

N-糖苷酶 F, 缩氨酸-N-糖苷酶F, 肽N-糖苷酶

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About This Item

UNSPSC代码:
41131616

重组

expressed in E. coli

质量水平

偶联物

(N-linked)

等级

Proteomics Grade

形式

ready-to-use solution

运输

wet ice

储存温度

2-8°C

一般描述

肽-N-糖苷酶F(PNGase F)属于酶家族,主要用于N-连接聚糖的去糖基化。

应用

PNGase Fast可用于固定以进行去糖基化。它也可用于固定在基于甲基丙烯酸酯的整体载体上,以从糖蛋白释放N-连接的碳水化合物部分。

生化/生理作用

肽-N-糖苷酶F(PNGase F)从糖蛋白上裂解天冬酰胺连接的高甘露糖,杂合和复杂寡糖。它也可以使天冬酰胺脱氨基为天冬氨酸。PNGase Fast能够对抗体和免疫球蛋白融合蛋白,以及其他糖蛋白进行完整和快速的去糖基化,以准备用于下游层析或质谱分析。PNGase Fast创建了优化的工作流程,在不损害灵敏度或重现性的情况下减少了处理时间。

WGK

WGK 3

法规信息

常规特殊物品

分析证书(COA)

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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
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)
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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