| Concentration | ≥2.5 U/mL |
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| Enzyme Applications|MultiLine | Preparation of deglycosylated proteins for molecular weight estimation or crystallography studies|Release of intact N-linked glycans from glycopeptides and glycoproteins|Structure and function studies of N-glycosylated glycoproteins| |
| Enzyme Formulation | 20 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA (pH 7.5) |
| Enzyme Source | Recombinant gene from Elizabethkingia meningoseptica, expressed in E. coli. The source organism was previously known as Chryseobacterium [Flavobacterium] meningosepticum. The enzyme is also known as PNGase F, peptide-N-glycosidase F, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase. |
| Enzyme Specific Activity | ≥10 units/mg |
| Enzyme Specificity | Cleaves all N-linked complex, hybrid or high mannose oligosaccharides, unless α(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. This product is Endo F free. |
| Enzyme 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. |
Answer:It cleaves the connection between an N-linked glycan's innermost GlcNAc and the peptide-bound asparagine.
Answer:The package supplies 80 µL at ≥2.5 U/mL, totaling 200 mU.
Answer:The package includes reaction buffer, denaturation solution, detergent solution and Tris reaction buffer for MS workflows.
AdvanceBio N-Glycanase (PNGase F), ≥2.5 U/mL is designed for enzymatic release of intact N-linked glycans from glycoproteins and glycopeptides for glycan profiling and protein characterization. This AdvanceBio N-Glycanase preparation contains recombinant peptide-N-glycosidase F (PNGase F), an enzyme that cleaves the linkage between the innermost N-acetylglucosamine of an N-linked glycan and its peptide-bound asparagine. The enzyme releases complex, hybrid and high-mannose N-glycans, except certain structures with α(1–3) core fucosylation. The preparation is endoglycosidase F-free and is derived from a recombinant gene expressed in Escherichia coli. This format supplies 80 µL at a concentration of at least 2.5 U/mL, equivalent to 200 mU per package. It includes 5× N-glycanase reaction buffer, denaturation solution, detergent solution and a 5× Tris reaction buffer for mass-spectrometry applications. The formulation contains 20 mM Tris-HCl, 50 mM NaCl and 1 mM EDTA at pH 7.5. The enzyme's optimal pH is 8.6 and its applicable pH range is 7.5–9.5. These components support preparation of deglycosylated proteins, assessment of N-linked glycan composition and structure–function experiments, including sample preparation before downstream glycan analysis.
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| Molecular Weight | ~35,000 daltons |
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| Unit | 200 mU |
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| Volume | 80 µL |
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| pH Optimum | 8.6 |
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| pH Range | 7.5-9.5 |
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