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NGLYF-RO

Roche

N-Glycosidase F

PNGase F of Flavobacterium meningosepticum, recombinant from E. coli

Sinônimo(s):

glycosidase

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About This Item

Número da licença da enzima:
3.5.1.52 (BRENDA, IUBMB)
Código UNSPSC:
12352204

recombinante

expressed in E. coli

Nível de qualidade

100

conjugado

(N-linked)

Ensaio

≥90% (SDS-PAGE)

forma

solution

atividade específica

~25000 units/mg protein

embalagem

pkg of 0.1 mL (11365169001 [100 U])
pkg of 0.25 mL (11365177001 [250 U])

fabricante/nome comercial

Roche

pH ideal

7.0-8.0

temperatura de armazenamento

−20°C

Categorias relacionadas

Descrição geral

Peptide-N-glycosidase F, Peptide-N4-(acetyl-β-glucosaminyl)-asparagine amidase

Aplicação

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.

Definição da unidade

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.

forma física

Solution in 50 mM sodium phosphate, 12.5 mM EDTA, 50% glycerol (v/v), pH 7.2

Outras notas

For life science research only. Not for use in diagnostic procedures.

Informações legais

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.

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

No data available

Ponto de fulgor (°C)

No data available

Certificados de análise (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

Protocolos

N-Glycosidase F Protocol & Troubleshooting

N-Glycosidase F Protocol & Troubleshooting

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