G8031
Glycopeptidase F from Elizabethkingia meningoseptica
buffered aqueous glycerol solution
别名:
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.
法规信息
新产品
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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
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
Dolores Linde et al.
Bioresource technology, 109, 123-130 (2012-02-03)
The extracellular β-fructofuranosidase Xd-INV from the yeast Xanthophyllomyces dendrorhous mainly synthesizes the neo-fructooligosaccharides (neo-FOS) neokestose and neonystose. This enzyme is a glycoprotein with a content of 59-67% N-linked carbohydrates and an estimated molecular mass of 160-200 kDa. The extent level
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
Ulla-Maja Bailey et al.
Journal of proteome research, 11(11), 5376-5383 (2012-10-09)
Asparagine-linked glycosylation is a common post-translational modification of proteins in eukaryotes. Mutations in the human ALG3 gene cause changed levels and altered glycan structures on mature glycoproteins and are the cause of a severe congenital disorder of glycosylation (CDG-Id). Diverse
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