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Merck

F8435

Sigma-Aldrich

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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About This Item

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

Key Documents

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Product Name

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

recombinant

expressed in E. coli

Quality Level

200

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

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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.

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. It was used to treat a purified protein, mouse cone ultraviolet (MUV) pigment, before use in quantitative immunoblot analysis in a study 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.

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.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

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
SLBX6198
SLBW0907
SLBC9416V
SLBC6287

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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
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
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
Ulla-Maja Bailey et al.
Journal of proteome research, 11(11), 5376-5383 (2012-10-09)
Asparagine-linked glycosylation is a common post-translational modification of proteins in eukaryotes. Mutations in the human ALG3 gene cause changed levels and altered glycan structures on mature glycoproteins and are the cause of a severe congenital disorder of glycosylation (CDG-Id). Diverse
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