NGLYF-RO
Roche
N-Glycosidase F
PNGase F of Flavobacterium meningosepticum, recombinant from E. coli
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recombinant
expressed in E. coli
Quality Level
conjugate
(N-linked)
Assay
≥90% (SDS-PAGE)
form
solution
specific activity
~25000 units/mg protein
packaging
pkg of 0.1 mL (11365169001 [100 U])
pkg of 0.25 mL (11365177001 [250 U])
manufacturer/tradename
Roche
optimum pH
7.0-8.0
storage temp.
−20°C
Related Categories
General description
Peptide-N-glycosidase F, Peptide-N4-(acetyl-β-glucosaminyl)-asparagine amidase
Application
Use N-glycosidase F to cleave all types of asparagine-bound N-glycans, provided that the amino group as well as the carboxyl group are present in a peptide linkage, and that the oligosaccharide has the minimum length of the chitobiose core unit. The reaction products are ammonia, aspartic acid (in the peptide chain), and the complete oligosaccharide.
Note: N-Glycosidase F, recombinant is also available as a lyophilizate without glycerol.
Note: N-Glycosidase F, recombinant is also available as a lyophilizate without glycerol.
Unit Definition
One unit is the enzyme activity which hydrolyzes 1 nmol dabsyl fibrin glycopeptide or 0.2 nmol dansyl fetuin glycopeptide within 1 minute at 37 °C at pH 7.8.
Physical form
Solution in 50 mM sodium phosphate, 12.5 mM EDTA, 50% glycerol (v/v), pH 7.2
Other Notes
For life science research only. Not for use in diagnostic procedures.
Legal Information
The sale of the Product does not exhaust or grant any rights in third party patents including patents of companies of the F. Hoffmann - La Roche AG group of companies, in particular, for the use of modified antibodies obtained by using the product.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
No data available
Flash Point(C)
No data available
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Ewoud van Tricht et al.
Talanta, 144, 1030-1035 (2015-10-11)
Current methods for the identification and/or quantification of viral proteins in influenza virus and virosome samples suffer from long analysis times, limited protein coverage and/or low accuracy and precision. We studied and optimized capillary gel electrophoresis (CGE) in order to
Fabian Higel et al.
mAbs, 6(4), 894-903 (2014-05-23)
N-glycosylation is a complex post-translational modification with potential effects on the efficacy and safety of therapeutic proteins and known influence on the effector function of biopharmaceutical monoclonal antibodies (mAbs). Comprehensive characterization of N-glycosylation is therefore important in biopharmaceutical development. In
Gerard Ja Rouwendal et al.
mAbs, 8(1), 74-86 (2015-10-07)
Monomeric IgA has been proposed as an alternative antibody format for cancer therapy. Here, we present our studies on the production, purification and functional evaluation of anti-HER2 IgA antibodies as anti-cancer agents in comparison to the anti-HER2 IgG1 trastuzumab. MALDI-TOF
Protocols
N-Glycosidase F Protocol & Troubleshooting
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