E2264
Endoglycosidase F3 from Elizabethkingia miricola
recombinant, expressed in E. coli, 30 U/mg
동의어(들):
Elizabethkingia miricola, Endo-β-N-acetylglucosaminidase F3, Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
Specific activity:
30 U/mg
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
Quality Level
conjugate
(N-linked)
form
solution
specific activity
30 U/mg
mol wt
32 kDa
shipped in
wet ice
storage temp.
2-8°C
Application
Endoglycosidase F3 from Elizabethkingia miricola has been used to analyze core fucosylation and tryptic digests of serum proteins.
Biochem/physiol Actions
Cleaves asparagine-linked biantennary and triantennary complex, oligosaccharides depending on the state of core fucosylation and peptide linkage.
Endoglycosidase F3 belongs to the glycoside hydrolase family 18 (GH18). It has hydrolytic activity. Endoglycosidase F3 glycosylates α-1,6-fucosylated GlcNAc derivative to give natural, core fucosylated complex-type N-glycopeptides.
Packaging
Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5
Physical form
Aseptically filled solution in 20 mM Tris-HCl, pH 7.5
Other Notes
One unit will release N-linked oligosaccharides from 1 μmole of denatured porcine fibrinogen in 1 minute at 37 °C, pH 4.5.
저장 등급
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Advances in Carbohydrate Chemistry (2016)
Chemical Biology of Glycoproteins (2017)
Liwei Cao et al.
Nature communications, 13(1), 3910-3910 (2022-07-08)
Core fucosylation of N-linked glycoproteins has been linked to the functions of glycoproteins in physiological and pathological processes. However, quantitative characterization of core fucosylation remains challenging due to the complexity and heterogeneity of N-linked glycosylation. Here we report a mass
Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM
Ma J, et al.
Journal of proteomics, 189, 67-74 (2018)
Characterization of novel endo-beta-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
Huang Y, et al.
Scientific reports, 8(1), 246-246 (2018)
문서
Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.
관련 콘텐츠
Instructions
자사의 과학자팀은 생명 과학, 재료 과학, 화학 합성, 크로마토그래피, 분석 및 기타 많은 영역을 포함한 모든 과학 분야에 경험이 있습니다..
고객지원팀으로 연락바랍니다.