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P7367

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

BioReagent, ≥95% (SDS-PAGE), for proteomics

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Synonym(s):
N-Glycosidase F, PNGase F from Chryseobacterium meningosepticum, PNGase F from Flavobacterium meningosepticum, Peptide N-glycosidase
CAS Number:
83534-39-8
Enzyme Commission number:
3.5.1.52 (BRENDA, IUBMB)
MDL number:
MFCD00131222
NACRES:
NA.32

biological source

bacterial (Elizabethkingia meningoseptica)

Quality Level

200

conjugate

(N-linked)

grade

for proteomics

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

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This Item
G1549F8435G0535
PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE), for proteomics

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

PNGase F from Elizabethkingia meningoseptica ready-to-use solution, recombinant, expressed in E. coli

Sigma-Aldrich

G1549

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

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

Sigma-Aldrich

G0535

Glycopeptidase A from almonds

grade

for proteomics

grade

Proteomics Grade

grade

Proteomics Grade

grade

-

assay

≥95% (SDS-PAGE)

assay

-

assay

-

assay

-

form

powder

form

ready-to-use solution

form

lyophilized powder

form

buffered aqueous glycerol solution

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

shelf life

≥1 yr at -20 °C

shelf life

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

shelf life

-

mol wt

~36 kDa

mol wt

~36 kDa

mol wt

~36 kDa

mol wt

-

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.

Application

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

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.

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.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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
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
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
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
Mikael B L Winkler et al.
Cell, 179(2), 485-497 (2019-09-24)
Niemann-Pick type C (NPC) proteins are essential for sterol homeostasis, believed to drive sterol integration into the lysosomal membrane before redistribution to other cellular membranes. Here, using a combination of crystallography, cryo-electron microscopy, and biochemical and in vivo studies on the
View All Related Papers

Articles

Post Translational Modification

Post-translational modifications such as glycosylation, phosphorylation, and sulfation, to name a few, serve many functions. As a result, the analysis of proteins and their post-translational modifications is particularly important for the study of diseases where multiple genes are known to be involved, such as heart disease, cancer and diabetes.

Strategies for Deglycosylating N-Linked Glycans

Explore various strategies for deglycosylating N-linked glycans involving PNGase F, PNGase A (Glycopeptidase A), and even native and sequential deglycosylation with endoglycosidases like Endoglycosidase H, Endoglycosidase F, and exoglycosidases.

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