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| Product Name | alpha2-3,6,8 Neuraminidase |
| Catalog No. | IVDRM-0306 |
| Description | alpha2-3,6,8 Neuraminidase, also termed a sialidase, is produced by recombinant expression in E. coli from a gene derived from Clostridium perfringens. The enzyme catalyses hydrolysis of sialic acids joined through alpha2-3, alpha2-6 and alpha2-8 linkages on both glycoproteins and free oligosaccharides, which makes it a standard tool for desialylating glycan substrates before structural analysis or further enzymatic digestion. |
| Intended Use | Removal of terminal sialic acids from glycoproteins and oligosaccharides prior to glycan analysis or downstream enzymatic steps. |
| Principle / Technology | The enzyme hydrolyses the ketosidic linkage between terminal sialic acid residues and the underlying galactose or N-acetylgalactosamine, releasing free Neu5Ac from alpha2-3, alpha2-6 and alpha2-8 linked substrates. |
| Detection Method | Terminal alpha2-3, alpha2-6 and alpha2-8 linked sialic acids |
| Sample Type | Glycoproteins, glycopeptides and oligosaccharides |
| Performance Range / Specifications | Supplied at 50 U per uL with purity above 90 percent by SDS-PAGE; consistent lot-to-lot performance confirmed with a fluorogenic sialic acid substrate. |
| Specificity | Hydrolyses alpha2-3, alpha2-6 and alpha2-8 sialyl linkages; no activity toward other glycosidic linkages is stated on the source record. |
| Reaction Conditions / Protocol | Combine glycoprotein or oligosaccharide substrate with the enzyme in the supplied 10x reaction buffer and incubate at 37°C until terminal sialic acids are released; proceed immediately to the chosen analytical method. |
| Components / Formulation | alpha2-3,6,8 Neuraminidase at 50 U per uL; 10x neuraminidase reaction buffer. Volumes scale with the selected pack size. |
| Storage Conditions | -25 to -15°C |
| Shelf Life | 12 months |
| Package Specifications | 2000 U or 10000 U packs including matched reaction buffer |
| Product Form | Liquid enzyme supplied with reaction buffer |
| Quality Control | Purity verified by SDS-PAGE (greater than 90 percent); activity confirmed against a fluorogenic sialylated substrate for every lot. |
| Key Features | Broad alpha2-3, alpha2-6 and alpha2-8 linkage coverage in a single enzyme; recombinant production ensures lot consistency. |
| Purity | >90% (SDS-PAGE) |
| Concentration | 50 U/uL |
| Activity / Unit Definition | One unit hydrolyses 1 nmol of Neu5Ac from an alpha2-3 linked sialyl trisaccharide substrate within 5 minutes at 37°C in a 10 uL reaction. |
| Source / Origin | Recombinant expression in E. coli; gene from Clostridium perfringens |
| pH Range / Optimal pH | 8.0 (storage buffer) |
| Shipping Conditions | Cold pack |
| Expiration Date / Stability | Stable for the full shelf life when held at the recommended storage temperature. |
| Regulatory / Compliance | For research and diagnostic reagent use; manufactured under controlled conditions with lot-specific release testing. |
| Compatibility | Compatible with glycan labelling, HPLC and mass spectrometric workflows after desialylation. |
| Recommended Buffer System | 20 mM Tris, 50 mM NaCl, 5 mM EDTA, pH 8.0 |
| Application Notes / Precautions | Verify linkage requirements for the substrate; alpha2-8 and alpha2-9 rich substrates may require the broader specificity enzyme variant. |
| Batch-to-Batch Consistency | Each lot is released with activity and purity documentation; lot number is printed on the vial label. |
| Delivery Standard | Cold pack dispatch by default |
| Turnaround Time | Standard dispatch |
| Readouts / Downstream Assays | SDS-PAGE, fluorogenic sialic acid assays, released glycan profiling |
For in vitro diagnostic use.
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