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Merck

P7367

PNGase F from Elizabethkingia meningoseptica

BioReagent, ≥95% (SDS-PAGE)

Sinónimos:

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

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About This Item

Número CAS:
83534-39-8
UNSPSC Code:
12352204
NACRES:
NA.32
Número CE:
3.5.1.52 (BRENDA, IUBMB)
MDL number:
MFCD18839214

Nombre del producto

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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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.

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

Clase de almacenamiento

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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Certificados de análisis (COA)

Lot/Batch Number
0000517842
0000517842
0000492644
0000492644
0000425209

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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
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
Giel Detienne et al.
Experimental gerontology, 60, 129-135 (2014-12-03)
Royalactin is a glycoprotein essential for the development of long-lived queen honeybees. Only larvae fed with royal jelly, containing royalactin, develop into queens. Royalactin plays a central role in this process by switching on the epidermal growth factor (EGF) receptor
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
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