324725
Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli
Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli cleaves asparagine-linked or free oligomannose and hybrid. Suitable for deglycosylation of native proteins.
동의어(들):
Endo-β-N-acetylglucosaminidase F1, Endo F1
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모든 사진(1)
About This Item
추천 제품
재조합
expressed in E. coli
Quality Level
결합
(N-linked)
형태
liquid
특이 활성도
≥16 units/mg protein
≥17 units/mL
제조업체/상표
Calbiochem®
저장 조건
do not freeze
외래 활성
Proteases, none detected
배송 상태
wet ice
저장 온도
2-8°C
일반 설명
Note: 1 mU = 1 milliunit.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F1 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and hybrid, but not complex oligosaccharides. Core fucosylation reduces activity by 50 fold. Endo F1 will hydrolyze sulfate containing high mannose chains. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore is more suitable for deglycosylation of native proteins.
Recombinant, Elizabethkingia meningosepticum endoglycosidase F1 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and hybrid, but not complex oligosaccharides. Core fucosylation reduces activity by 50 fold. Endo F1 will hydrolyze sulfate containing high mannose chains. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185), and therefore is more suitable for deglycosylation of native proteins.
경고
Toxicity: Standard Handling (A)
단위 정의
One unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1.0 µmol denatured ribonuclease B per min at 37°C, pH 5.5.
물리적 형태
In 20 mM Tris-HCl, pH 7.5.
기타 정보
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
법적 정보
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
The Journal of biological chemistry, 267(6), 3868-3872 (1992-03-06)
A full-length insert for the endo-beta-N-acetylglucosaminidase (Endo) F1 gene was located on a 2,200-base pair EcoRI fragment of genomic DNA and cloned into the plasmid vector Bluescript. Transformed Escherichia coli cells expressed Endo F1 activity very well, but the enzyme
The Journal of biological chemistry, 266(3), 1646-1651 (1991-01-25)
Flavobacterium meningosepticum endo-beta-acetyl-glucosaminidase F preparations have been resolved by hydrophobic interaction chromatography on TSK-butyl resin into at least three activities designated endo F1, endo F2 and endo F3 each with a unique substrate specificity. The 32-kDa endo F1 protein is
Nature communications, 13(1), 6325-6325 (2022-10-25)
The ability to reconstitute natural glycosylation pathways or prototype entirely new ones from scratch is hampered by the limited availability of functional glycoenzymes, many of which are membrane proteins that fail to express in heterologous hosts. Here, we describe a
Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum.
Methods in enzymology, 230, 44-57 (1994-01-01)
문서
Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.
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