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Merck
CN

A0810

内切糖苷酶H 来源于褶皱链霉菌

recombinant, expressed in E. coli, buffered aqueous solution

别名:

β-N-乙酰氨基葡萄糖苷酶 H

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
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产品名称

内切糖苷酶H 来源于褶皱链霉菌, recombinant, expressed in E. coli, buffered aqueous solution

recombinant

expressed in E. coli

conjugate

(N-linked)

form

buffered aqueous solution

shipped in

wet ice

storage temp.

2-8°C

Quality Level

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Biochem/physiol Actions

糖苷内切酶H参与裂解高甘露糖型糖中聚糖链核心中两个N-乙酰氨基葡萄糖(GlcNAc)残基之间的N-连接的聚糖。

General description

糖苷内切酶H或称内切β-N-乙酰氨基葡萄糖苷酶H是一种糖水解酶。它由褶皱链霉菌和其它链霉菌种产生。

Other Notes

在37℃、pH5.5条件下,一个单位可在每分钟内从1 μmole变性核糖核酸酶B中释放N-连接的寡糖。

Physical form

溶于含有50 nM NaCl、1 mM EDTA的20mM Tris-HCl,pH 7.5溶液

wgk

WGK 1

存储类别

12 - Non Combustible Liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

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分析证书(COA)

Lot/Batch Number

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High-Level Expression of Endo-
Freeze H H and Kranz C
Current Protocols in Molecular Biology, 0 17(3) (2010)
High-Level Expression of Endo-
Wang F, et al.
Testing, 10(3) (2015)
Ulla-Maja Bailey et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 923-924, 16-21 (2013-03-05)
Post-translational modification of proteins with glycosylation is of key importance in many biological systems in eukaryotes, influencing fundamental biological processes and regulating protein function. Changes in glycosylation are therefore of interest in understanding these processes and are also useful as
T Tai et al.
The Journal of biological chemistry, 250(21), 8569-8575 (1975-11-10)
Heterogeneities of the two ovalbumin glycopeptides, (Man)5(GlcNAc)2Asn and (Man)6(GlcNAc)2Asn, were revealed by borate paper electrophoresis of oligosaccharide alcohols obtained from the glycopeptides by endo-beta-N-acetylglucosaminidase H digestion and NaB3H4 reduction. The structures of the major components of the oligosaccharides were determined
Endo-beta-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae.
N Koide et al.
The Journal of biological chemistry, 249(15), 4897-4904 (1974-08-10)

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

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