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P9120

Sigma-Aldrich

PNGase F from Elizabethkingia meningoseptica

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

Synonyme(s) :

N-Glycosidase F, PNGase F, Peptide N-glycosidase

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About This Item

Numéro CAS:
83534-39-8
Numéro de classification (Commission des enzymes):
3.5.1.52 (BRENDA, IUBMB)
Numéro MDL:
MFCD00131222
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli

Niveau de qualité

200

Conjugué

(N-linked)

Activité spécifique

≥10 units/mg protein

Poids mol.

36 kDa

Conditionnement

set of 100 units nanomolar unit

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Application

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

PNGase F is a glycosylasparaginase used to deglycosylate proteins. It is widely used in structure-function studies of glycoproteins.
Produit utilisé pour la déglycosylation des protéines.

Actions biochimiques/physiologiques

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.
Clive un glycane entier d′une glycoprotéine, à condition que le fragment d′asparagine glycosylé soit substitué sur ses extrémités amino et carboxyle avec une chaîne polypeptidique.

Conditionnement

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

Définition de l'unité

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.

Informations légales

N-Glycanase is a registered trademark of Agilent Technologies Inc

Mention d'avertissement

Danger

Classification des risques

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

Code de la classe de stockage

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

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
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)
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
Amelie Croset et al.
Journal of biotechnology, 161(3), 336-348 (2012-07-21)
Glycosylation is one of the most common posttranslational modifications of proteins. It has important roles for protein structure, stability and functions. In vivo the glycostructures influence pharmacokinetics and immunogenecity. It is well known that significant differences in glycosylation and glycostructures
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