G8031
Glycopeptidase F from Elizabethkingia meningoseptica
buffered aqueous glycerol solution
Synonym(s):
N-Glycosidase F, PNGase F, Peptide N-glycosidase
form
buffered aqueous glycerol solution
shipped in
dry ice
storage temp.
−20°C
Application
Used to deglycosylate protein.
Physical form
Solution in 50% glycerol containing 100 mM sodium phosphate, 25 mM EDTA and 5 mM sodium azide, pH 7.2
Other Notes
1 unit is the enzyme activity which hydrolyzes 1 nmole dabsyl fibrin glycopeptide within 1 minute at 37°C and pH 7.8.
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Hui Zhou et al.
Analytical biochemistry, 427(1), 33-35 (2012-04-21)
Common de-N-glycosylation protocols usually require a lengthy incubation time. Although pressure cycling technology or scientific microwave reactors can accelerate this enzyme reaction, they may not be easily accessible. In this brief report, we employed an alternative strategy using a standard
Helle Malerod et al.
Journal of proteome research, 12(1), 248-259 (2012-12-05)
The adenocarcinoma cell line HeLa serves as a model system for cancer research in general and cervical cancer in particular. In this study, hydrazide enrichment in combination with state-of-the art nanoLC-MS/MS analysis was used to profile N-linked glycosites in HeLa
Yukiko Kamiya et al.
FEBS letters, 586(8), 1141-1146 (2012-05-12)
PUB domains are identified in several proteins functioning in the ubiquitin (Ub)-proteasome system and considered as p97-binding modules. To address the further functional roles of these domains, we herein characterized the interactions of the PUB domain of peptide:N-glycanase (PNGase) with
Anuradha Gosain et al.
BMC biochemistry, 13, 9-9 (2012-06-12)
Peptide: N- glycanase (PNGase) enzyme cleaves oligosaccharides from the misfolded glycoproteins and prepares them for degradation. This enzyme plays a role in the endoplasmic reticulum associated degradation (ERAD) pathway in yeast and mice but its biological importance and role in
A plant peptide: N-glycanase orthologue facilitates glycoprotein ER-associated degradation in yeast.
Yuki Masahara-Negishi et al.
Biochimica et biophysica acta, 1820(10), 1457-1462 (2012-06-05)
The cytoplasmic peptide:N-glycanase (PNGase) is a deglycosylating enzyme involved in the ER-associated degradation (ERAD) process, while ERAD-independent activities are also reported. Previous biochemical analyses indicated that the cytoplasmic PNGase orthologue in Arabidopsis thaliana (AtPNG1) can function as not only PNGase
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service