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P7367

PNGase F from Elizabethkingia meningoseptica

BioReagent, ≥95% (SDS-PAGE)

Synonym(s):

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

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50 UNITS

€370.00

300 UNITS

€1,710.00

€370.00

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About This Item

CAS Number:
83534-39-8
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
3.5.1.52 (BRENDA, IUBMB)
MDL number:
MFCD18839214
Assay:
≥95% (SDS-PAGE)
Biological source:
bacterial (Elizabethkingia meningoseptica)
Concentration:
≥300 units/mL
≥50 units/mL

Key Documents

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Product Name

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

biological source

bacterial (Elizabethkingia meningoseptica)

conjugate

(N-linked)

product line

BioReagent

assay

≥95% (SDS-PAGE)

form

powder

shelf life

≥1 weeks at 2‑8 °C (for a reconstituted solution >500 units/ml)
≥1 yr at 2‑8 °C
Solution is stable for at least 3 freeze-thaw cycles

mol wt

~36 kDa

concentration

≥300 units/mL
≥50 units/mL

optimum pH

~8.6

shipped in

wet ice

storage temp.

2-8°C

Quality Level

200

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1 of 4

This Item
F8435P9120G0535
PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE)

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

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

Glycopeptidase A from almonds buffered aqueous glycerol solution, ≥0.05 unit/mL

Sigma-Aldrich

G0535

Glycopeptidase A from almonds

biological source

bacterial (Elizabethkingia meningoseptica)

biological source

-

biological source

-

biological source

-

grade

for proteomics

grade

Proteomics Grade

grade

-

grade

-

assay

≥95% (SDS-PAGE)

assay

-

assay

-

assay

-

form

powder

form

lyophilized powder

form

-

form

buffered aqueous glycerol solution

concentration

≥300 units/mL, ≥50 units/mL

concentration

-

concentration

-

concentration

≥0.05 unit/mL

shelf life

≥1 weeks at 2‑8 °C (for a reconstituted solution >500 units/ml), Solution is stable for at least 3 freeze-thaw cycles, ≥1 yr at 2‑8 °C

shelf life

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

shelf life

-

shelf life

-

Application

PNGase F from Elizabethkingia meningoseptica has been used:
  • for de-N-glycosylation of Zika20virus E protein[1]
  • to evaluate coxsackievirus and adenovirus receptor glycosylation using CAR-expressing COS cells[2]
  • to verify the N-linked glycosylation of MHC class 1 polypeptide-related sequence A (MICA)[3]

Suitable for both proteomics and glycobiology use; compatible with MALDI-TOF MS analysis
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.

General description

Proteomics Grade PNGase F has been extensively purified and lyophilized from dilute potassium phosphate buffer to produce a stable product. The product is free from glycerol and other stabilizers, and contains very low levels of buffer salts. This highly purified material is excellent for N-linked deglycosylation of glycoproteins or glycopeptides in gel, in solution, or on blot membranes.

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

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

13 - Non Combustible Solids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000517842
0000517842
0000425209
0000425209
0000324090

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Terry Nguyen-Khuong et al.
Glycoconjugate journal, 35(6), 499-509 (2018-11-24)
Analysis of glycans via a porous graphitized carbon liquid chromatography (PGC-LC) coupled with electrospray ionization (tandem) mass spectrometry (ESI-MS(/MS)) is a powerful analytical method in the field of glycomics. Isobaric glycan structures can be identified reliably with the help of
Mikkel G Terp et al.
NPJ precision oncology, 5(1), 65-65 (2021-07-17)
EGFR tyrosine kinase inhibitor (TKI) resistance in non-small cell lung cancer (NSCLC) patients is inevitable. Identification of resistance mechanisms and corresponding targeting strategies can lead to more successful later-line treatment in many patients. Using spectrometry-based proteomics, we identified increased fibroblast
Daniel Nouri-Nejad et al.
Molecular biology of the cell, 32(5), 376-390 (2021-01-07)
Pannexin 1 (PANX1) is a glycoprotein that forms large pore channels capable of passing ions and metabolites such as ATP for cellular communication. PANX1 has been implicated in many diseases including breast cancer and melanoma, where inhibition or deletion of
Lars Andresen et al.
Journal of immunology (Baltimore, Md. : 1950), 188(4), 1847-1855 (2012-01-10)
NKG2D ligand surface expression is important for immune recognition of stressed and neotransformed cells. In this study, we show that surface expression of MICA/B and other NKG2D ligands is dependent on N-linked glycosylation. The inhibitor of glycolysis and N-linked glycosylation
Katherine J D Ashbourne Excoffon et al.
Journal of virology, 81(11), 5573-5578 (2007-03-23)
The coxsackievirus and adenovirus receptor (CAR) is both a viral receptor and homophilic adhesion protein. The extracellular portion of CAR consists of two immunoglobulin (Ig)-like domains, each with a consensus sequence for N-glycosylation. We used chemical, genetic, and biochemical studies
View All Related Papers

Articles

Post Translational Modification

Protein modifications are crucial for disease study. Analysis methods are key.

Strategies for Deglycosylating N-Linked Glycans

Explore strategies for releasing N-linked glycans with PNGase F, PNGase A & native & sequential deglycosylation with endoglycosidases & exoglycosidases.

Protocols

Mass Spectrometry of Glycans

Explore mass spectrometry analysis of glycans for glycomic & glycoproteomic neutral & acidic glycan analysis. See a general mass spec glycan analysis procedure.

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