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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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1 KIT
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About This Item

UNSPSC代码:
41131616

$713.00

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重组

expressed in E. coli

质量水平

200

偶联物

(N-linked)

等级

Proteomics Grade

表单

ready-to-use solution

运输

wet ice

储存温度

2-8°C

相关类别

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。[1]

应用

PNGase Fast可用于固定以进行去糖基化。[1]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。[2]

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，[3]杂合和复杂寡糖。它也可以使天冬酰胺脱氨基为天冬氨酸。[4]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。

储存分类代码

10 - Combustible liquids

历史批次信息供参考:

分析证书(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
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
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
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)
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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