E7642
内切糖苷酶H 来源于褶皱链霉菌
recombinant, expressed in E. coli, buffered aqueous solution
别名:
β-N-乙酰氨基葡萄糖苷酶 H
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关于此项目
recombinant
expressed in E. coli
form
buffered aqueous solution
mol wt
27 kDa
storage temp.
2-8°C
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.
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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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)
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
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.
Shu-Quan Fan et al.
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
Francesco Renzi et al.
PLoS pathogens, 7(6), e1002118-e1002118 (2011-07-09)
C. canimorsus 5 has the capacity to grow at the expenses of glycan moieties from host cells N-glycoproteins. Here, we show that C. canimorsus 5 also has the capacity to deglycosylate human IgG and we analyze the deglycosylation mechanism. We
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