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
MDL number:
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
conjugate
(N-linked)
form
buffered aqueous solution
shipped in
wet ice
storage temp.
2-8°C
Quality Level
Related Categories
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.
Physical form
Solution in 20 mM Tris HCl, pH 7.5, containing 50 mM NaCl, 1 mM EDTA
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.
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)
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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)
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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