One microspin column of Immobilized PNGase F contains sufficient material for removal of N-glycans from 0.2 mg glycoprotein. PNGase F is an amidase that digests the bond between the innermost GlcNAc of N-glycans and asparagine residues on the glycoprotein backbone. It is active on high-mannose, hybrid and complex-type N-glycans.
| Product Group | |
|---|---|
| Source/Origin | Recombinant and engineered enzyme from E. meningoseptica, Produced in E. coli (His-tagged), 36 kDa |
| Product Composition | |
| Digestion Site | |
| Specificity | |
| Substrates | |
| Reaction Conditions | |
| Digestion Buffers | |
| Buffer Compatibility | Lower yield in 20 mM Tris pH 8.6 and in PBS. 0. 15M NaCl in buffers recommended. |
| Inhibitors | |
| Unit Definition | |
| Application | N-glycan analysis and profiling and sample deglycosylation prior to analysis. |
The columns are recommended to be used for deglycosylation at native conditions only.
PNGase F Immobilized hydrolyzes the amide bond between the polypeptide asparagine and the innermost GlcNAc of all mammalian asparagine-linked complex, hybrid, or high mannose oligosaccharides. It does not remove N-glycans with α1-3 core fucosylation.
No, it is not recommended. We can only guarantee optimal performance for one-time use.
Yes! Contact us at info@genovis.com
The recommended buffer for best performance of the column is TBS buffer at pH 8.6. Other buffers with neutral pH containing 0.15 M NaCl can also be used but optimization may then be required.
