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| Product Name | PNGase F with Polyhistidine Tag, 100000 U/mL (15000 U / 75000 U) |
| Catalog No. | IVDRM-0299 |
| Description | Peptide-N-glycosidase F is the standard route to stripping every N-linked glycan from a glycoprotein in one step. This preparation is produced recombinantly in yeast at a specific activity of 100000 units per millilitre and acts on high-mannose, hybrid and complex structures alike. It hydrolyses the amide bond between the innermost N-acetylglucosamine and the asparagine residue, converting that asparagine to aspartic acid in the process, so the mass shift observed downstream reflects both the loss of the glycan and the single-residue conversion. A polyhistidine tag is present for removal afterwards. The kit supplies three companion solutions: a denaturing buffer carrying detergent and dithiothreitol, a Tris buffer at pH 7.5, and a non-ionic detergent solution. |
| Intended Use | Complete removal of N-linked glycans from antibodies and other glycoproteins before mass spectrometry, electrophoretic mobility analysis or glycan profiling. |
| Principle / Technology | The amidase releases the whole glycan from the peptide backbone by cleaving the bond linking the reducing-end sugar to the amide nitrogen of asparagine. |
| Detection Method | Released glycans and the deglycosylated protein are examined by chromatography, electrophoresis or mass spectrometry. |
| Sample Type | Purified glycoproteins, monoclonal antibodies and glycosylated protein fragments. |
| Performance Range / Specifications | 100000 units per millilitre; acts on high-mannose, hybrid and complex N-linked structures; complete deglycosylation of antibodies; polyhistidine tag aids removal; three companion buffers supplied. |
| Sensitivity / LOD | Does not apply; sensitivity comes from the downstream detection chemistry. |
| Specificity | Molecular weight 36 kDa; specific activity 100000 units per millilitre; supplied as 15000 U or 75000 U with denaturing buffer, Tris buffer at pH 7.5 and non-ionic detergent solution. |
| Reaction Conditions / Protocol | Denature the glycoprotein in the detergent and dithiothreitol buffer, cool, add Tris buffer at pH 7.5 with non-ionic detergent, add the enzyme and incubate at 37 °C, then analyse directly. |
| Components / Formulation | Enzyme solution plus denaturing buffer, Tris buffer at pH 7.5 and non-ionic detergent solution. |
| Storage Conditions | Store at -25 to -15 °C. |
| Shelf Life | 1 year from receipt when stored as recommended. |
| Package Specifications | Enzyme supplied at 15000 U or 75000 U with matched buffer volumes. |
| Product Form | Liquid enzyme in glycerol-containing buffer with three companion solutions. |
| Quality Control | Each lot is calibrated by unit activity against denatured RNase B as the reference substrate. |
| Key Features | - 100000 units per millilitre for strong deglycosylation capacity - Handles high-mannose, hybrid and complex N-linked structures - Unit definition anchored to denatured RNase B - Polyhistidine tag allows removal after digestion - Three companion buffers included for the standard workflow |
| Purity | Recombinant glycosidase free of contaminating protease activity. |
| Concentration | 100000 units per millilitre. |
| Activity / Unit Definition | One unit removes more than 95% of carbohydrate from 10 ug of denatured RNase B in one hour at 37 °C in a 10 uL reaction. |
| Molecular Weight | 36 kDa. |
| Source / Origin | Recombinantly expressed in yeast with a polyhistidine tag. |
| pH Range / Optimal pH | Storage and reaction buffer is 20 mM Tris-HCl at pH 7.5 with 50 mM sodium chloride, 5 mM EDTA and 50% glycerol. |
| Shipping Conditions | Shipped cold. |
| Expiration Date / Stability | Remains usable for the full shelf life provided the temperature recommendation is followed. |
| Regulatory / Compliance | For research use only. |
| Compatibility | Glycerol-containing storage buffer suits general glycosylation analysis; where an HPLC or mass application is affected by glycerol, a glycerol-free formulation should be selected. |
| Recommended Buffer System | 20 mM Tris-HCl at pH 7.5, 50 mM sodium chloride, 5 mM EDTA and 50% glycerol. |
| Application Notes / Precautions | Denaturation of the substrate is normally required for complete glycan release, and the asparagine-to-aspartate conversion must be accounted for when interpreting mass shifts. |
| Batch-to-Batch Consistency | Lot-to-lot consistency is maintained through defined manufacturing specifications; every lot ships with its release record. |
| Model Type | Complete N-deglycosylation enzyme |
| Starting Material / Tissue Site | Yeast-expressed recombinant amidase with a polyhistidine tag |
| Delivery Standard | Enzyme vial plus three buffer vials |
| Turnaround Time | dispatch is arranged at order confirmation. |
| Readouts / Downstream Assays | Mass shift of the protein and identity of released glycans by downstream analysis. |
For in vitro diagnostic use.
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