N-Glycosidase F
ROCHE/NGLYFL-RO - recombinant form of the gene from Flavobacterium meningosepticum
Synonym: N-Glycosidase F; PNGase F; Peptide-
Product Type: Chemical
| assay | ≥90% (SDS-PAGE) |
| biological source | bacterial ( |
| color | colorless |
| conjugate | (N-linked) |
| foreign activity | Endoglycosidase F |
| a-Fucosidase, present | |
| b-Galactosidase, present | |
| b-N-Acetylhexosaminidase, present | |
| dA(17h ≤100 units, present | |
| form | lyophilized |
| manufacturer/tradename | Roche |
| mol wt | 35.5 kDa |
| optimum pH | 7.0-8.0 |
| packaging | pkg of 100 U (11365185001) |
| pkg of 250 U (11365193001) | |
| purified by | electrophoresis |
| Quality Level | 100  |
| recombinant | expressed in E. coli |
| solubility | water: soluble |
| specific activity | >25000 units/mg protein |
| storage condition | ( |
| storage temp. | 2-8°C |
| suitability | suitable for enzyme test |
| technique(s) | activity assay: suitable |
| 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. |
| 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. |
| Other Notes: | For life science research only. Not for use in diagnostic procedures. |
| 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. |
| 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. |
| 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. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 2 |
| Flash Point(F) | does not flash |
| Flash Point(C) | does not flash |
| Purity | ≥90% (SDS-PAGE) |
| activity | specific activity: >25000 units/mg protein |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 3.5.1.52 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352200 |