PNGase F
Recombinant Glycosidase Cloned from <i>Elizabethkingia miricola</i>
- Use to determine protein glycosylation status and location
- Cleaves N-linked oligosaccharides between innermost GlcNAc and asparagines from N-linked glycoproteins
- Will not remove oligosaccharides found on plant glycoproteins
- Supplied at a concentration of 10u/μl
Catalog Number:
Size
Catalog Number: V4831
PNGase F, Recombinant Glycosidase
PNGase F is a recombinant glycosidase cloned from Elizabethkingia miricola and overexpressed in E. coli. PNGase F has a molecular weight of 36kDa. PNGase F catalyzes the cleavage of N-linked oligosaccharides between the innermost GlcNAc and asparagine residues of high mannose, hybrid and complex oligosaccharides from N-linked glycoproteins (see figure). PNGase F will not remove oligosaccharides containing Alpha-(1,3)-linked core fucose commonly found on plant glycoproteins.
Unit Definition: One unit of PNGase F will catalyze the deglycosylation of 1 nanomole of denatured Ribonuclease B (RNase B) in one minute at 37°C. One Promega unit is equal to 1 IUB milliunit.
Molecular Weight: PNGase F has a molecular weight of approximately 36kDa.
Physical Form: PNGase F is supplied as a liquid in 20mM Tris-HCl (pH 7.5 at 25°C), 50mM NaCl and 5mM EDTA at a concentration of 10,000u/ml.
Applications- Characterizing whether the protein is glycosylated
- Determining the location of glycosylation on the protein
- Characterizing the glycan structure
- Protein trafficking
Twenty micrograms of various denatured glycoprotein standards were treated with 10 units of Promega recombinant or native PNGase F for 1 hour at 37°C. Gel shifts indicating deglycosylation were monitored by SDS-PAGE.
Protocols
Complete Protocol
Specifications
Catalog Number:
Contenido
| Item | Part # | Presentación | Concentración |
|---|---|---|---|
PNGase F |
V483A | 1 × 500 units | 10u/μl |
SDS
Search for SDSCertificado de Análisis
Use Restrictions
For Research Use Only. Not for Use in Diagnostic Procedures.Condiciones de Almacenaje
Resources
No related resources available
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