G1549
PNGase F Glycosidase
de-glycosylates N-linked glycoproteins for analysis, suitable for mass spectrometry, recmobinant, expressed in E. coli
Synonyme(s) :
N-Glycosidase F, PNGase F, Peptide N-glycosidase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥1000 U/mg
Recombinant:
expressed in E. coli
Shelf life:
≥1 yr at -20 °C
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Laissez-nous vous aiderNom du produit
PNGase F from Elizabethkingia meningoseptica, ready-to-use solution, recombinant, expressed in E. coli
recombinant
expressed in E. coli
conjugate
(N-linked)
grade
Proteomics Grade
form
ready-to-use solution
specific activity
≥1000 U/mg
shelf life
≥1 yr at -20 °C
mol wt
~36 kDa
shipped in
wet ice
storage temp.
−20°C
Quality Level
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Application
Produit utilisé pour la déglycosylation des protéines.
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.
Biochem/physiol Actions
Clive un glycane entier d′une glycoprotéine, à condition que le fragment d′asparagine glycosylé soit substitué sur ses extrémités amino et carboxyle avec une chaîne polypeptidique.
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.
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.
Physical form
Supplied as 300 Units/mL enzyme in 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5.
Classe de stockage
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
Characterization and analysis of extracellular matrix in malignant brain tumors and their cellular derivatives
Extracellular Matrix, 113-138 (2015)
N-glycosylation of apolipoprotein A1 in cardiovascular diseases
Majek P, et al.
Translational Research, 165(2), 360-362 (2015)
Proteome changes of plasma-derived extracellular vesicles in patients with myelodysplastic syndrome.
Klara Pecankova et al.
PloS one, 17(1), e0262484-e0262484 (2022-01-11)
Extracellular vesicles are released into body fluids from the majority of, if not all, cell types. Because their secretion and specific cargo (e.g., proteins) varies according to pathology, extracellular vesicles may prove a rich source of biomarkers. However, their biological
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