E7642
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
recombinant
expressed in E. coli
form
buffered aqueous solution
mol wt
27 kDa
storage temp.
2-8°C
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Unit Definition
One unit will hydrolyze 1.0 μmole of dabsyl-Asn-(GlcNAc)2(Man)5 per min at pH 5.5 at 37 °C.
Physical form
Solution in 0.05 M sodium phosphate, pH 7, containing 25 mM EDTA and preservative
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Rhizomucor miehei aspartic proteinases having improved properties.
Advances in experimental medicine and biology, 436, 293-296 (1998-04-30)
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.
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
The Journal of biological chemistry, 287(14), 11272-11281 (2012-02-10)
Endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae (Endo-D) is an endoglycosidase capable of hydrolyzing the Fc N-glycan of intact IgG antibodies after sequential removal of the sialic acid, galactose, and internal GlcNAc residues in the N-glycan. Endo-D also possesses transglycosylation activity with sugar
The Journal of biological chemistry, 285(41), 31348-31361 (2010-07-20)
γ-aminobutyric acid type A (GABA(A)) receptors are heteropentameric glycoproteins. Based on consensus sequences, the GABA(A) receptor β2 subunit contains three potential N-linked glycosylation sites, Asn-32, Asn-104, and Asn-173. Homology modeling indicates that Asn-32 and Asn-104 are located before the α1
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