G1549

PNGase F Glycosidase

de-glycosylates N-linked glycoproteins for analysis, suitable for mass spectrometry, recmobinant, expressed in E. coli

• Sinonimo/i: PNGase F from Elizabethkingia meningoseptica, N-Glycosidase F, PNGase F from Chryseobacterium meningosepticum, PNGase F from Flavobacterium meningosepticum, Peptide N-glycosidase
• Numero CAS: 83534-39-8
• UNSPSC Code: 12352204
• NACRES: NA.54
• Numero CE: 3.5.1.52 (BRENDA, IUBMB)
• MDL number: MFCD18839214

Proprietà

• Nome del prodotto: PNGase F from Elizabethkingia meningoseptica, ready-to-use solution, recombinant, expressed in E. coli
• recombinant: expressed in E. coli
• conjugate: (N-linked)
• grade: Proteomics Grade
• form: ready-to-use solution
• specific activity: ≥1000 U/mg
• shelf life: ≥1 yr at -20 °C
• mol wt: ~36 kDa
• shipped in: wet ice
• storage temp.: −20°C
• Quality Level: 200

Descrizione

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[1] and in deglycosylation of chondroitin sulfate proteoglycan.[2]

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.

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.[3] It is cost-effectively produced on a large scale in prokaryotic hosts and requires divalent zinc ions for its enzymatic activity.[4]

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.

Informazioni sulla sicurezza

• Classe di stoccaggio: 10 - Combustible liquids
• wgk: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable