324727
Endoglycosidase F3, Elizabethkingia meningosepticum, Recombinant, E. coli
Endoglycosidase F3, Elizabethkingia meningosepticum, Recombinant, E. coli, cleaves asparagine-linked or free biantennary and triantennary complex, and Man3GlcNAc oligosaccharides from glycoproteins.
동의어(들):
Endo-β-N-acetylglucosaminidase F3, Endo F3
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모든 사진(1)
About This Item
추천 제품
재조합
expressed in E. coli
Quality Level
결합
(N-linked)
양식
liquid
특이 활성도
≥30 units/mg protein
≥5 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
Recombinant, Elizabethkingia meningosepticum endoglycosidase F3 expressed in E. coli. Cleaves asparagine-linked or free biantennary and triantennary complex, and Man3GlcNAc oligosaccharides from glycoproteins. This enzyme 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 residue. Core fucosylation increases the activity of Endo F3 up to 40 fold. Exhibits no activity on high mannose and hybrid molecules. 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 F3 expressed in E. coli. Cleaves asparagine-linked or free biantennary and triantennary complex, and Man3GlcNAc oligosaccharides from glycoproteins. This enzyme 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 residue. Core fucosylation increases the activity of Endo F3 up to 40 fold. Exhibits no activity on high mannose and hybrid molecules. 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 porcine fibrinogen per min at 37°C, pH 5.5.
기타 정보
Tarentino, A.L., et al. 1995. Glycobiology 5, 599.
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1993. J. Biol. Chem. 268, 9702.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1993. J. Biol. Chem. 268, 9702.
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.
A L Tarentino et al.
The Journal of biological chemistry, 268(13), 9702-9708 (1993-05-05)
The genes for Flavobacterium meningosepticum Endo (endoglycosidase) F2 and Endo F3 were cloned, and their nucleotide sequences were determined. The deduced amino acid sequences were verified independently to a large extent by direct peptide microsequencing of 66 and 84% of
A L Tarentino et al.
Glycobiology, 5(6), 599-601 (1995-09-01)
The gene for endo-beta-N-acetylglucosaminidase F3 was cloned into the high-expression vector pMAL c-2, and expressed in Escherichia coli as a fusion protein. A key step in the purification employed Poros II (HS) chromatography, which greatly facilitated isolation of the enzyme
R B Trimble et al.
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
Enzymatic deglycosylation of asparagine-linked glycans: purification, properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum.
A L Tarentino et al.
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.
자사의 과학자팀은 생명 과학, 재료 과학, 화학 합성, 크로마토그래피, 분석 및 기타 많은 영역을 포함한 모든 과학 분야에 경험이 있습니다..
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