E7642
Endoglycosidase H from Streptomyces plicatus
recombinant, expressed in E. coli, buffered aqueous solution
Synonym(s):
β-N-Acetylglucosaminidase H
recombinant
expressed in E. coli
form
buffered aqueous solution
mol wt
27 kDa
storage temp.
2-8°C
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Physical form
Solution in 0.05 M sodium phosphate, pH 7, containing 25 mM EDTA and preservative
Other Notes
One unit will hydrolyze 1.0 μmole of dabsyl-Asn-(GlcNAc)2(Man)5 per min at pH 5.5 at 37 °C.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Rhizomucor miehei aspartic proteinases having improved properties.
M K Harboe
Advances in experimental medicine and biology, 436, 293-296 (1998-04-30)
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
Yusuke Tomabechi et al.
Carbohydrate research, 345(17), 2458-2463 (2010-10-12)
To determine the structural specificity of the glycosyl acceptor of the transglycosylation reaction using endo-β-N-acetylglucosaminidase (ENGase) (EC 3.2.1.96) from Mucor hiemalis (Endo-M), several acceptor derivatives were designed and synthesized. The narrow regions of the 1,3-diol structure from the 4- to
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
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