์ฝ˜ํ…์ธ ๋กœ ๊ฑด๋„ˆ๋›ฐ๊ธฐ
Merck

324725

Endoglycosidase F1

Cleaves specific N-glycan structures, suitable for Mass Spectrometry, from Elizabethkingia meningosepticum, recombinant, expressed in E. coli

๋™์˜์–ด(๋“ค):

Endo-β-N-acetylglucosaminidase F1, Endo F1

์กฐ์ง ๋ฐ ๊ณ„์•ฝ ๊ฐ€๊ฒฉ์„ ๋ณด๋ ค๋ฉด ๋กœ๊ทธ์ธ๋ฅผ ํด๋ฆญํ•ฉ๋‹ˆ๋‹ค.

ํฌ๊ธฐ ์„ ํƒ


์ œํ’ˆ์ •๋ณด (DICE ๋ฐฐ์†ก ์‹œ ๋น„์šฉ ๋ณ„๋„)

EC ๋ฒˆํ˜ธ:
UNSPSC Code:
12352202
NACRES:
NA.54
Specific activity:
≥16 units/mg protein
≥17 units/mL
Recombinant:
expressed in E. coli
๊ธฐ์ˆ  ์„œ๋น„์Šค
๋„์›€์ด ํ•„์š”ํ•˜์‹ ๊ฐ€์š”? ์ €ํฌ ์ˆ™๋ จ๋œ ๊ณผํ•™์ž ํŒ€์ด ๋„์™€๋“œ๋ฆฌ๊ฒ ์Šต๋‹ˆ๋‹ค.
๋„์›€ ๋ฌธ์˜
๊ธฐ์ˆ  ์„œ๋น„์Šค
๋„์›€์ด ํ•„์š”ํ•˜์‹ ๊ฐ€์š”? ์ €ํฌ ์ˆ™๋ จ๋œ ๊ณผํ•™์ž ํŒ€์ด ๋„์™€๋“œ๋ฆฌ๊ฒ ์Šต๋‹ˆ๋‹ค.
๋„์›€ ๋ฌธ์˜

์ œํ’ˆ ์ด๋ฆ„

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.

recombinant

expressed in E. coli

conjugate

(N-linked)

form

liquid

specific activity

≥16 units/mg protein
≥17 units/mL

manufacturer/tradename

Calbiochemยฎ

storage condition

do not freeze

foreign activity

Proteases, none detected

shipped in

wet ice

storage temp.

2-8ยฐC

Quality Level

General description

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.

Disclaimer

Toxicity: Standard Handling (A)

Other Notes

One unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1.0 ยตmol denatured ribonuclease B per min at 37ยฐC, pH 5.5.
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.

Physical form

In 20 mM Tris-HCl, pH 7.5.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

์ €์žฅ ๋“ฑ๊ธ‰

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


์‹œํ—˜ ์„ฑ์ ์„œ(COA)

์ œํ’ˆ์˜ ๋กœํŠธ/๋ฐฐ์น˜ ๋ฒˆํ˜ธ๋ฅผ ์ž…๋ ฅํ•˜์—ฌ ์‹œํ—˜ ์„ฑ์ ์„œ(COA)์„ ๊ฒ€์ƒ‰ํ•˜์‹ญ์‹œ์˜ค. ๋กœํŠธ ๋ฐ ๋ฐฐ์น˜ ๋ฒˆํ˜ธ๋Š” ์ œํ’ˆ ๋ผ๋ฒจ์— ์žˆ๋Š” โ€˜๋กœํŠธโ€™ ๋˜๋Š” โ€˜๋ฐฐ์น˜โ€™๋ผ๋Š” ์šฉ์–ด ๋’ค์—์„œ ์ฐพ์„ ์ˆ˜ ์žˆ์Šต๋‹ˆ๋‹ค.

์ด ์ œํ’ˆ์„ ์ด๋ฏธ ๊ฐ€์ง€๊ณ  ๊ณ„์‹ญ๋‹ˆ๊นŒ?

๋ฌธ์„œ ๋ผ์ด๋ธŒ๋Ÿฌ๋ฆฌ์—์„œ ์ตœ๊ทผ์— ๊ตฌ๋งคํ•œ ์ œํ’ˆ์— ๋Œ€ํ•œ ๋ฌธ์„œ๋ฅผ ์ฐพ์•„๋ณด์„ธ์š”.

๋ฌธ์„œ ๋ผ์ด๋ธŒ๋Ÿฌ๋ฆฌ ๋ฐฉ๋ฌธ

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

๋ฌธ์„œ

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

๊ตญ์ œ ๋ฌด์—ญ ํ’ˆ๋ชฉ ๋ฒˆํ˜ธ

SKUGTIN
324725-700MIUCN04055977215991

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