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F8435

PNGase F Glycosidase

Removes N-linked glycans, suitable for mass spectrometry, recombinant, expressed in E. coli

Synonym(s):

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

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50 UNITS

€229.00

300 UNITS

€1,080.00

€229.00

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About This Item

CAS Number:
83534-39-8
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
3.5.1.52 (BRENDA, IUBMB)
MDL number:
MFCD18839214

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Product Name

PNGase F from Elizabethkingia meningoseptica, lyophilized powder, recombinant, expressed in E. coli

recombinant

expressed in E. coli

conjugate

(N-linked)

grade

Proteomics Grade

form

lyophilized powder

specific activity

≥1,000 U/mg

shelf life

≥1 weeks at 2‑8 °C (for reconstituted solution)
≥1 yr at -20 °C

mol wt

~36 kDa

shipped in

wet ice

storage temp.

−20°C

Quality Level

200

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This Item
P9120P7367362185
PNGase F from Elizabethkingia meningoseptica lyophilized powder, recombinant, expressed in E. coli

Sigma-Aldrich

F8435

PNGase F from Elizabethkingia meningoseptica

PNGase F from Elizabethkingia meningoseptica recombinant, expressed in E. coli, set of 100 units nanomolar unit

Sigma-Aldrich

P9120

PNGase F from Elizabethkingia meningoseptica

PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE)

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

N-Glycosidase F, Elizabethkingia meningosepticum

Sigma-Aldrich

362185

N-Glycosidase F, Elizabethkingia meningosepticum

grade

Proteomics Grade

grade

-

grade

for proteomics

grade

-

specific activity

≥1,000 U/mg

specific activity

≥10 units/mg protein

specific activity

-

specific activity

≥20,000 units/mg protein, ≥4500 units/mL

form

lyophilized powder

form

-

form

powder

form

liquid

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

recombinant

-

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Application

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-teminal 6x histidine fusion tag.
Used to deglycosylate protein.

Biochem/physiol Actions

Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.

Other Notes

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.

Packaging

PNGase F was used for deglycosylation of P-glycoprotein in a study to investigate the dual impact of statins on p-glycoprotein and its effect on doxorubicin cytotoxicity in human neuroblastoma cells.[1] It was used to treat a purified protein, mouse cone ultraviolet (MUV) pigment, before use in quantitative immunoblot analysis in a study[2] It is used to deglycosylate N-linked glycoproteins. 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-teminal 6x histidine fusion tag.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000432197
0000432197
0000405902
0000405900
0000405900

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Maria Nordgren et al.
Methods in molecular biology (Clifton, N.J.), 2271, 155-167 (2021-04-29)
O-glycosylation is a difficult posttranslational modification to analyze. O-glycans are labile and often cluster making their analysis by LC-MS very challenging. OpeRATOR is an O-glycan specific protease that cleaves the protein backbone N-terminally of glycosylated serine and threonine residues. This
Tobias Bierig et al.
Frontiers in bioengineering and biotechnology, 8, 618615-618615 (2021-01-08)
2019-nCoV is the causative agent of the serious, still ongoing, worldwide coronavirus disease (COVID-19) pandemic. High quality recombinant virus proteins are required for research related to the development of vaccines and improved assays, and to the general understanding of virus
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
Evelyn Sieczkowski et al.
International journal of cancer, 126(9), 2025-2035 (2009-09-10)
The development of multidrug resistance (MDR) is a major problem during cancer treatment. Drug efflux via ATP-binding cassette (ABC) transporters is the main mechanism responsible for resistance to chemotherapeutics. We have recently observed that statins enhance susceptibility to doxorubicin-induced apoptosis
Lauren L Daniele et al.
Investigative ophthalmology & visual science, 46(6), 2156-2167 (2005-05-26)
To test the hypothesis that Nrl(-)(/)(-) photoreceptors are cones, by comparing them with WT rods and cones using morphological, molecular, histochemical, and electrophysiological criteria. The photoreceptor layer of fixed retinal tissue of 4- to 6-week-old mice was examined in plastic
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