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Merck

P9120

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

recombinant, expressed in E. coli, set of 100 units nanomolar unit

Synonym(s):

N-Glycanase®, 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

Pricing and availability is not currently available.

recombinant

expressed in E. coli

Quality Level

conjugate

(N-linked)

specific activity

≥10 units/mg protein

mol wt

36 kDa

packaging

set of 100 units nanomolar unit

shipped in

wet ice

storage temp.

2-8°C

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This Item
G1549F8435P7367
recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

mol wt

36 kDa

mol wt

~36 kDa

mol wt

~36 kDa

mol wt

~36 kDa

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

Application

PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation
  • of recombinant soybean agglutinin (rSBA) in Nicotiana benthamiana (NbrSBA) and Solanum tuberosum (StrSBA)[1]
  • of frontal cortical lysate to verify the glycosylation profile of β-secretase (BACE proteins)[2]
  • of cell lysate for evaluating the siRNA silencing of cellular prion protein (PrPc) post transfection[3]

PNGase F is a glycosylasparaginase used to deglycosylate proteins. It is widely used in structure-function studies of glycoproteins[4].
Used to deglycosylate protein.

Biochem/physiol Actions

PNGase F 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 deaminates the asparagine to aspartic acid, but leaves the oligosaccharide intact. PNGase F will not remove oligosaccharides containing α(1-3)-linked core fucose, commonly found in plant glycoproteins. A tripeptide with the oligosaccharide-linked asparagine as the central residue is the minimal substrate for PNGase F[4].
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.

Packaging

Each set includes enzyme, two formulations of 5× reaction buffer (for routine and mass spectrometry downstream analysis), detergent and denaturation solutions

Unit Definition

One unit will catalyze the release of N-linked oligosaccharides from 1 micromole 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.

Legal Information

N-Glycanase is a registered trademark of Agilent Technologies Inc

Signal Word

Danger

Hazard Classifications

Acute Tox. 3 Dermal - Acute Tox. 4 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - Eye Dam. 1 - Repr. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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PrPc activation induces neurite outgrowth and differentiation in PC12 cells: role for caveolin-1 in the signal transduction pathway
Pantera B, et al.
Journal of Neurochemistry, 110(1), 194-207 (2009)
G E Norris et al.
Structure (London, England : 1993), 2(11), 1049-1059 (1994-11-15)
Peptide:N-glycosidase F (PNGase F) is an enzyme that catalyzes the complete removal of N-linked oligosaccharide chains from glycoproteins. Often called an endoglycosidase, it is more correctly termed an amidase or glycosylasparaginase as cleavage is at the asparagine-sugar amide linkage. The
Mitochondrial respiratory inhibition and oxidative stress elevate beta-secretase (BACE1) proteins and activity in vivo in the rat retina
Xiong K, et al.
Experimental Brain Research. Experimentelle Hirnforschung. Experimentation Cerebrale, 181(3), 435-446 (2007)
Reynald Tremblay et al.
Transgenic research, 20(2), 345-356 (2010-06-19)
Soybean agglutinin (SBA) is a specific N-acetylgalactosamine-binding plant lectin that can agglutinate a wide variety of cells. SBA has great potential for medical and biotechnology-focused applications, including screening and treatment of breast cancer, isolation of fetal cells from maternal blood
Anna C Need et al.
Journal of medical genetics, 49(6), 353-361 (2012-05-15)
There is considerable interest in the use of next-generation sequencing to help diagnose unidentified genetic conditions, but it is difficult to predict the success rate in a clinical setting that includes patients with a broad range of phenotypic presentations. The

Articles

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

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

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

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

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