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.
Szinonimák:
Endo-β-N-acetylglucosaminidase F1, Endo F1
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Javasolt termékek
rekombináns
expressed in E. coli
Minőségi szint
konjugátum
(N-linked)
form
liquid
specifikus aktivitás
≥16 units/mg protein
≥17 units/mL
gyártó/kereskedő neve
Calbiochem®
tárolási körülmény
do not freeze
idegen aktivitás
Proteases, none detected
kiszállítva
wet ice
tárolási hőmérséklet
2-8°C
Related Categories
Általános leírás
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.
Figyelmeztetés
Toxicity: Standard Handling (A)
Egység definíció
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.
Fizikai forma
In 20 mM Tris-HCl, pH 7.5.
Egyéb megjegyzések
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.
Jogi információk
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
A L Tarentino et al.
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
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)
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
Thapakorn Jaroentomeechai et al.
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
Cikkek
Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.
Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.
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