E0639
内切糖苷酶F2 from Elizabethkingia miricola
recombinant, expressed in E. coli, 20 U/mg
别名:
内-β-N-乙酰氨基葡糖苷酶F2，Endo F2, 内切糖苷酶F2 来源于脑膜炎脓毒性黄杆菌, 内切糖苷酶F2 来源于脑膜脓毒性伊丽莎白菌, 内切糖苷酶F2 来源于脑膜脓毒性金黄杆菌, 米尔伊丽莎白菌
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包装
提供 5× 反应缓冲液，250 mM 醋酸钠，pH 4.5
外形
无菌灌装溶液，含10 mM乙酸钠、25 mM氯化钠，pH 4.5
其他说明
一个单元将在37 °C、pH 4.5下每分钟从1 μmole变性猪纤维蛋白原释放N-连接寡糖。
储存分类代码
10 - Combustible liquids
WGK
nwg
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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
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
Wen-Yi Lo et al.
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
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
商品
Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.
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