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Merck

G1549

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

ready-to-use solution, recombinant, expressed in E. coli

Synonim(y):

PNGase F from Elizabethkingia meningoseptica, N-Glycosidase F, PNGase F from Chryseobacterium meningosepticum, PNGase F from Flavobacterium meningosepticum, Peptide N-glycosidase

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About This Item

Numer CAS:
Numer EC enzymu:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54

rekombinowane

expressed in E. coli

Poziom jakości

białko sprzężone

(N-linked)

klasa czystości

Proteomics Grade

Postać

ready-to-use solution

aktywność właściwa

≥1000 U/mg

okres trwałości

≥1 yr at -20 °C

masa cząsteczkowa

~36 kDa

Warunki transportu

wet ice

temp. przechowywania

−20°C

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Zastosowanie

Recombinant PNGase F has been purified by affinity chromatography and dialyzed into a 50% glycerol solution with 10 mM potassium phoosphate pH 7.5 to produce a stable product. The product contains low levels of buffer salts. This highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-terminal 6x histidine fusion tag. PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation assay in human plasma samples and in deglycosylation of chondroitin sulfate proteoglycan.
Used to deglycosylate protein.

Działania biochem./fizjol.

PNGase F from Elizabethkingia meningoseptica has glycan-binding catalytic domain and a bowl-like domain at the N-terminus. It cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain. It is cost-effectively produced on a large scale in prokaryotic hosts and requires divalent zinc ions for its enzymatic activity.
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.

Definicja jednostki

One unit will catalyze the release of N-linked oligosaccharides from 1 nanomole of denatured ribonuclease B in one minute at 37°C at pH 7.5 monitored by SDS-PAGE. One Sigma unit of PNGase F activity is equal to 1 IUB milliunit.

Postać fizyczna

Supplied as 300 Units/mL enzyme in 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5.
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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

N-glycosylation of apolipoprotein A1 in cardiovascular diseases
Majek P, et al.
Translational Research, 165(2), 360-362 (2015)
Characterization and analysis of extracellular matrix in malignant brain tumors and their cellular derivatives
Extracellular Matrix, 113-138 (2015)
Discovery and characterization of a novel extremely acidic bacterial N-glycanase with combined advantages of PNGase F and A
Wang T, et al.
Bioscience Reports, 34(6), e00149-e00149 (2014)
Identification and characterization of a novel prokaryotic peptide: N-glycosidase from Elizabethkingia meningoseptica
Sun G, et al.
The Journal of Biological Chemistry, jbc-M114 (2015)
T H Plummer et al.
The Journal of biological chemistry, 259(17), 10700-10704 (1984-09-10)
Endo-beta-N-acetylglucosaminidase F preparations from Flavobacterium meningosepticum have been found to contain peptide:N-glycosidase activity. Only the second activity, designated as peptide:N-glycosidase F, readily cleaves the beta-aspartylglycosylamine linkage of a fetuin triantennary complex glycopeptide, as shown by the isolation of the corresponding

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