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

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About This Item

Enzyme Commission number:
3.5.1.52 (BRENDA, IUBMB)
UNSPSC Code:
12352204

biological source

bacterial (Flavobacterium meningosepticum)

Quality Level

100

recombinant

expressed in E. coli

conjugate

(N-linked)

Assay

≥90% (SDS-PAGE)

form

lyophilized

specific activity

>25000 units/mg protein

mol wt

35.5 kDa

purified by

electrophoresis

packaging

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

manufacturer/tradename

Roche

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

technique(s)

activity assay: suitable

color

colorless

optimum pH

7.0-8.0

solubility

water: soluble

suitability

suitable for enzyme test

foreign activity


Endoglycosidase F, none detected
a-Fucosidase, present
b-Galactosidase, present
b-N-Acetylhexosaminidase, present
dA(17h ≤100 units, present

storage temp.

2-8°C

Related Categories

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.

N-glycosidase F, also known as PNGase F, is an asparagine amidase enzyme derived from Flavobacterium meningosepticum. It is widely used as a valuable tool in protein research to investigate and analyze N-glycosylation.

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

N-Glycosidase F has been used for deglycosylation of N-glycoproteins.

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

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Highly efficient production of peptides: N-glycosidase F for N-glycomics analysis
Hua L, et al.
Protein Expression and Purification, 17-22 (2014)
Integrated proteomic, phosphoproteomic and N-glycoproteomic analyses of chicken eggshell matrix
Yang R, et al.
Food Chemistry, 330 (2020)
Xueyan Cao et al.
Food chemistry, 276, 266-273 (2018-11-10)
Milk glycoproteins are crucial nutrients with a variety of functions. However, whey N-glycoproteomes in human and bovine milks have not been characterized during lactation. Herein, using lectin enrichment and liquid chromatography tandem mass spectrometry, 68, 58, 100, and 98 N-glycoproteins
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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