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
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Related Categories
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. 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.
signalword
Danger
hcodes
pcodes
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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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
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
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
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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