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G1549

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

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

Synonym(s):

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

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

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

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Application

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.

Biochem/physiol Actions

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.

Unit Definition

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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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