PNGase F from Elizabethkingia meningoseptica
SIGMA/G1549 - ready-to-use solution, recombinant, expressed in E. coli
Synonym: PNGase F from Elizabethkingia meningoseptica; N-Glycosidase F; PNGase F from Chryseobacterium meningosepticum; PNGase F from Flavobacterium meningosepticum; Peptide N-glycosidase
CAS Number: 83534-39-8
MDL Number: MFCD18839214
Product Type: Chemical
Figure 4. Cleavage site and structural requirements for PNGase F.
R1 = N- and C-substitution by groups other than H
R2 = H or the rest of an oligosaccharide structure
R3 = H or α(1→6)fucose
R1 = N- and C-substitution by groups other than H
R2 = H or the rest of an oligosaccharide structure
R3 = H or α(1→6)fucose
| conjugate | (N-linked) |
| form | ready-to-use solution |
| grade | Proteomics Grade |
| mol wt | ~36 kDa |
| Quality Level | 200  |
| recombinant | expressed in E. coli |
| shelf life | ≥1 yr at -20 °C |
| shipped in | wet ice |
| specific activity | ≥1000 U/mg |
| storage temp. | −20°C |
| Application: | Recombinant PNGase F has been purified by affinity chromatography and dialyzed into a 50% glycerol solution with 10 mM potassium phoosphate pH 7.5 to produce a stable product. The product contains low levels of buffer salts. This highly purified material can be used for preparative deglycosylation or for analytical applications in gel, in solution, or on blot membranes. The enzyme can be removed from preparative operations by utilizing its C-terminal 6x histidine fusion tag. PNGase F from Elizabethkingia meningoseptica has been used in deglycosylation assay in human plasma samples and in deglycosylation of chondroitin sulfate proteoglycan. |
| Application: | Used to deglycosylate protein. |
| Biochem/physiol Actions: | Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain. |
| Biochem/physiol Actions: | PNGase F from Elizabethkingia meningoseptica has glycan-binding catalytic domain and a bowl-like domain at the N-terminus. It cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain. It is cost-effectively produced on a large scale in prokaryotic hosts and requires divalent zinc ions for its enzymatic activity. |
| Other Notes: | One unit will catalyze the release of N-linked oligosaccharides from 1 nanomole of denatured ribonuclease B in one minute at 37°C at pH 7.5 monitored by SDS-PAGE. One Sigma unit of PNGase F activity is equal to 1 IUB milliunit. |
| Physical form: | Supplied as 300 Units/mL enzyme in 50% (v/v) glycerol and 50% (v/v) 20 mM Potassium Phosphate, pH 7.5. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥1000 U/mg |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.5.1.52 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |