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Merck
CN

A0810

Endoglycosidase H from Streptomyces plicatus

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

β-N-Acetylglucosaminidase H

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
MDL number:
Recombinant:
expressed in E. coli
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Product Name

Endoglycosidase H from Streptomyces plicatus, 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

Endoglycosidase H is involved in cleaving the N-linked glycans present between the two N-acetylglucosamine (GlcNAc) residues in the core of the glycan chain in high-mannose sugars.

General description

Endoglycosidase H or endo-β-N-acetylglucosaminidase H is an glycohydrolase. It is produced by Streptomyces plicatus and other Streptomyces species.

Other Notes

One unit will release N-linked oligosaccharides from 1 μmole of denatured ribonuclease B per min at 37 °C at pH 5.5.

Physical form

Solution in 20 mM Tris HCl, pH 7.5, containing 50 mM NaCl, 1 mM EDTA

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Regulatory Information

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High-Level Expression of Endo-
Wang F, et al.
Testing, 10(3) (2015)
High-Level Expression of Endo-
Freeze H H and Kranz C
Current Protocols in Molecular Biology, 0 17(3) (2010)
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
The release of intact oligosaccharides from specific glycoproteins by endo-beta-N-acetylglucosaminidase H.
A L Tarentino et al.
The Journal of biological chemistry, 249(3), 818-824 (1974-02-10)
Roger S Zou et al.
Aging, 3(10), 968-984 (2011-10-13)
A distinct conformational transition from the α-helix-rich cellular prion protein (PrPC) into its β-sheet-rich pathological isoform (PrPSc) is the hallmark of prion diseases, a group of fatal transmissible encephalopathies that includes spontaneous and acquired forms. Recently, a PrPSc-like intermediate form

Articles

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

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