表单
buffered aqueous glycerol solution
运输
dry ice
储存温度
−20°C
应用
Used to deglycosylate protein.
外形
Solution in 50% glycerol containing 100 mM sodium phosphate, 25 mM EDTA and 5 mM sodium azide, pH 7.2
其他说明
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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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
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
Yu-Chen Lee et al.
Methods in molecular biology (Clifton, N.J.), 909, 29-41 (2012-08-21)
Isolation of highly purified plasma membranes is the key step in constructing the plasma membrane proteome. Traditional plasma membrane isolation method takes advantage of the differential density of organelles. While differential centrifugation methods are sufficient to enrich for plasma membranes
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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