P9120
PNGase F from Elizabethkingia meningoseptica
recombinant, expressed in E. coli, set of 100 units nanomolar unit
Sinónimos:
PNGase F
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
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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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.
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.
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
signalword
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
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
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Los clientes también vieron
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)
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Pantera B, et al.
Journal of Neurochemistry, 110(1), 194-207 (2009)
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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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