Sialidase PRIME-LY
Cleaves α2,3-, α2,6- and α2,8- linked sialic acids
Made for removing silic acids from glycoconjugates
Sialidases are a family of exoglycosidases that catalyze the cleavage of non-reducing sialic acid residues of mono- or oligosaccharide chains on glycoconjugates. Sialidase PRIME-LY™ comes in a lyophilized form, which is perfectly suitable for solution-based analyses. This enzyme cleaves α2,3-, α2,6- and α2,8- linked sialic acids. Because of its broad substrate specificity, Sialidase PRIME-LY™ is capable of completely removing sialic acids from glycoconjugates of a wide variety of biological materials (cells, antibodies, serum, tissues etc.).
Sialidase PRIME-LY - Lyophillized
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SPECIFICATIONS
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| Part Numbers | NZSP010LY |
| Target | Asparagine-linked (N-linked) or serine/threonine linked (O-linked) oligosaccharides (complex/terminally sialyated) |
| Compatible Glycoprotein | Native an denatured |
| Biological Source | Recombinant, E. coli |
| Total Protocol Length | 30 minutes to 24 hours |
| Experiment Types | In vitro and in situ |
| Typical Yield | 1 Unit of enzyme will completely de-sialate 10 µg of denatured alpha 1 anti-trypsin following incubation for 10 minutes at 37°C. 1 Unit = 1 IUB milliunit. |
| Concentration | 50 Units/µL after resuspending in 100 µL of dH2O. |
| Purity | ≥95% as determined by SDS PAGE |
| Compatible with Mass Spec | Yes |
| Contains Glycerol | No |
| Affinity Tag for Purification | Yes. Sialidase PRIME-L contains a His-tag. |
| Storage | Supplied lyophilized and shipped at ambient temperature. Once reconstituted, store at -20°C or 4°C (avoid multiple freeze-thaws) |
| Shelf Life | 1 year |
| Microbe Free | Yes, lot tested |