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NGLYF-RO

Roche

N-Glycosidase F

PNGase F of Flavobacterium meningosepticum, recombinant from E. coli

Synonym(s):

glycosidase

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0.1 mL

Available to ship TODAYfromMILWAUKEE

$452.00
0.25 mL
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$821.00

About This Item

UNSPSC Code:
12352204
EC Number:
3.5.1.52 (BRENDA, IUBMB)
NACRES:
NA.54
Specific activity:
~25000 units/mg protein
Assay:
≥90% (SDS-PAGE)
Recombinant:
expressed in E. coli

$452.00

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recombinant

expressed in E. coli

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

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.[1][2][3] 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.

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.
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.

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.

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This Item
NGLYFL-ROP9120P7367
N-Glycosidase F PNGase F of Flavobacterium meningosepticum, recombinant from E. coli

Roche

NGLYF-RO

N-Glycosidase F

N-Glycosidase F recombinant form of the gene from Flavobacterium meningosepticum

Roche

NGLYFL-RO

N-Glycosidase F

PNGase F from Elizabethkingia meningoseptica recombinant, expressed in E. coli, set of 100 units nanomolar unit

Sigma-Aldrich

P9120

PNGase F from Elizabethkingia meningoseptica

PNGase F from Elizabethkingia meningoseptica BioReagent, ≥95% (SDS-PAGE)

Sigma-Aldrich

P7367

PNGase F from Elizabethkingia meningoseptica

specific activity

~25000 units/mg protein

specific activity

>25000 units/mg protein

specific activity

≥10 units/mg protein

specific activity

-

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

-

assay

≥95% (SDS-PAGE)

form

solution

form

lyophilized

form

-

form

powder

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

expressed in E. coli

recombinant

-

optimum pH

7.0-8.0

optimum pH

7.0-8.0

optimum pH

-

optimum pH

~8.6

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

No data available

flash_point_c

No data available

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Certificates of Analysis (COA)

Lot/Batch Number
58283320
46484723
16070925
82661420
58283326

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Protocols

N-Glycosidase F Protocol & Troubleshooting

N-Glycosidase F Protocol & Troubleshooting

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

Global Trade Item Number

SKUGTIN
1136517700104061838250780
1136516900104061838701350