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Specifications
- Enzyme type:Recombinant
- Source:E. coli
- Species:Elizabethkingia meningoseptica
- Size:400 µl (1 U)
- Enzyme name:N-Glycanase
- Enzyme synonyms:PNGase F
- Molecular weight:~35,000 daltons
- Concentration:≥2.5 U/mL
- Formulation:20 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA (pH 7.5)
- Tested applications:Release of intact N-linked glycans from glycopeptides and glycoproteins;Structure-function studies of N-glycosylated glycoproteins;Preparation of deglycosylated proteins for molecular weight estimation or crystallography studies
- Cat. no.:CAGKE-5006D
Specifications
About this item
AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/mL (formerly ProZyme). A recombinant form of PNGase F, releases intact N-glycans by cleaving between the innermost GlcNAc and Asn. Includes 5x N-glycanase reaction buffer, denaturation solution, detergent solution, 5x N-glycanase Tris reaction buffer (MS applications). Supplied at a concentration of ≥ 2.5 U/mL. For a more concentrated formulation of ≥ 10 U/mL, which may be useful for native digestions, see GKE-5010B or GKE-5020B (EDTA-free).
- pH range: 7.5-9.5 (Optimum: 8.6)
- Unit definition: One unit is defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 µmole of denatured ribonuclease B per minute at 37°C, pH 7.5.
Prepare samples for analytical methods by removing glycans or by deglycosylation of proteins.
These products are most commonly used to remove glycans for analysis, or to obtain deglycosylated proteins for analysis
Notable among these these is PNGase F, an asparagine amidase that releases intact N-glycans by cleaving between the innermost GlcNAc of the N-glycan and the asparagine (Asn) residue of the peptide the N-glycan is linked to.
Agilent Endoglycosidases (formerly ProZyme) release oligosaccharides from glycoproteins and some other substrates. These enzymes are useful for deglycosylating glycoproteins prior to analysis, or for releasing N-glycans for labeling and analysis. Useful in N-glycan analysis, Agilent offers PNGase F, an asparagine amidase that releases intact N-glycans. PNGase F cleaves between the innermost GlcNac of the N-glycan and the asparagine (Asn) residue of the peptide to which the N-glycan is linked.
Source: Recombinant gene from Elizabethkingia meningoseptica, expressed in E. coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum. Enzyme is also known as peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase.
Specificity: Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless a(1-3) core fucosylated, as in plant glycans and some insect glycans. Asparagine must be peptide bonded at both termini. Phosphate, sulfate and sialic acid groups attached to the oligosaccharide do not affect cleavage. Endo F free.