E6878
Endoglycosidase H from Streptomyces griseus
lyophilized powder
Synonym(s):
β-N-Acetylglucosaminidase H
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
Pricing and availability is not currently available.
form
lyophilized powder
shipped in
dry ice
storage temp.
−20°C
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Unit Definition
One unit will hydrolyze 1.0 μmole of N-acetyl-(14C)Asn(GlcNAc)2(Man)5 per min at pH 5.0 at 37 °C.
Physical form
Lyophilized powder containing bovine serum albumin
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Liv Anette Bøhle et al.
FEMS microbiology letters, 325(2), 123-129 (2011-11-19)
It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18 endoglycosidase domain and a GH20 domain.
Helena Ryšlavá et al.
The FEBS journal, 278(14), 2469-2484 (2011-05-14)
Fungal β-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group
Valentina Botti et al.
PloS one, 6(8), e23838-e23838 (2011-08-23)
Hepatitis C Virus E1E2 heterodimers are components of the viral spike. Although there is a general agreement on the necessity of the co-expression of both E1 and E2 on a single coding unit for their productive folding and assembly, in
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
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
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