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Merck

A0810

Sigma-Aldrich

Endoglycosidase H from Streptomyces plicatus

recombinant, expressed in E. coli, buffered aqueous solution

Sinónimos:

β-N-Acetylglucosaminidase H

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About This Item

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

recombinant

expressed in E. coli

conjugate

(N-linked)

form

buffered aqueous solution

shipped in

wet ice

storage temp.

2-8°C

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General description

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

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.

Unit Definition

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_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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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
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
Eric M Rubenstein et al.
The Journal of cell biology, 197(6), 761-773 (2012-06-13)
Little is known about quality control of proteins that aberrantly or persistently engage the endoplasmic reticulum (ER)-localized translocon en route to membrane localization or the secretory pathway. Hrd1 and Doa10, the primary ubiquitin ligases that function in ER-associated degradation (ERAD)
Midori Umekawa et al.
Biochimica et biophysica acta, 1800(11), 1203-1209 (2010-07-22)
An efficient method for synthesizing homogenous glycoproteins is essential for elucidating the structural and functional roles of glycans of glycoproteins. We have focused on the transglycosylation activity of endo-ß-N-acetylglucosaminidase from Mucor hiemalis (Endo-M) as a tool for glycoconjugate syntheses, since

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