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NGLYFL-RO

Roche

N-Glycosidase F

recombinant form of the gene from Flavobacterium meningosepticum

Synonym(s):
N-Glycosidase F, PNGase F
Enzyme Commission number:

conjugate

(N-linked)

Quality Level

Assay

≥90% (SDS-PAGE)

form

lyophilized

specific activity

>25000 units/mg protein

packaging

pkg of 100 U (11365185001)
pkg of 250 U (11365193001)

manufacturer/tradename

Roche

optimum pH

7.0-8.0

storage temp.

2-8°C

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This Item
NGLYF-RO10105031001BGALS-RO
N-Glycosidase F recombinant form of the gene from Flavobacterium meningosepticum

Roche

NGLYFL-RO

N-Glycosidase F

N-Glycosidase F PNGase F of Flavobacterium meningosepticum, recombinant from E. coli

Roche

NGLYF-RO

N-Glycosidase F

β-Galactosidase from E. coli overproducer

Roche

10105031001

β-Galactosidase

β-Glucuronidase from E. coli K 12

Roche

BGALS-RO

β-Glucuronidase

form

lyophilized

form

solution

form

suspension

form

solution

specific activity

>25000 units/mg protein

specific activity

~25000 units/mg protein

specific activity

~300 units/mg protein (At 37 °C with 2-nitrophenyl-β-D-galactoside as the substrate, approximately 30 U/mg at 25 °C with lactose as the substrate; standardized with BSA.)

specific activity

~80 units/mg protein (Glucuronidase at 25 °C, or 140 U/mg at 37 °C, at pH 7 with 4-nitrophenyl-β-D-glucuronide as substrate; 1 ml β-Glucuronidase contains at least 140 U at 37 °C.)

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

Roche

optimum pH

7.0-8.0

optimum pH

7.0-8.0

optimum pH

7

optimum pH

6.0-6.5

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

General description

N-Glycosidase F (PNGase F) is a potent enzyme which hydrolyzes at glycosylamine linkage. It also helps in generating a carbohydrate-free peptide and oligosaccharide with di-N-acetylchitobiose unit.
Peptide-N-glycosidase F, Peptide-N4-(acetyl-β-glucosaminyl)-asparagine amidase

Specificity

Hydrolyzes all types of N-glycan chains from glycopeptides and glycoproteins unless they carry α1,3-linked core fucose residues present in insect and plant glycoproteins. Free of contaminating proteolytic activities (x = H or sugar[s]) according to current quality control procedures.

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 solution.

Unit Definition

One unit is the enzyme activity which hydrolyzes 1 nmol dabsyl fibrin glycopeptide or 0.2 nmol dansyl fetuin glycoprotein within 1 minute at 37 °C and pH 7.8.

Physical form

Clear, colorless solution after reconstitution

Preparation Note

Storage conditions (working solution): 2 to 8 °C
The reconstituted solution is stable at 2 to 8 °C for at least four weeks.

Reconstitution

Dissolving the content in 0.1 ml redist water (100 unit package) or 0.25 ml double-dist. water (250 unit package) respectively, results in a concentration of 100 mM sodium phosphate buffer, 25 mM EDTA, pH 7.2.
Note: N-Glycosidase F, recombinant is also available as solution with 50% glycerol.

Other Notes

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

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 2

Flash Point(F)

does not flash

Flash Point(C)

does not flash


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Customers Also Viewed

A L Tarentino et al.
Biochemistry, 24(17), 4665-4671 (1985-08-13)
Endo-beta-N-acetylglucosaminidase F (Endo F) and peptide:N-glycosidase F (PNGase F) were purified from cultures of Flavobacterium meningosepticum by ammonium sulfate precipitation followed by gel filtration on TSK HW-55(S). This system separated the two enzymes and provided PNGase F in a high

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