![PNGase F (with His-tag)](https://user-images.strikinglycdn.com/res/hrscywv4p/image/upload/c_limit,fl_lossy,h_1000,w_500,f_auto,q_auto/2311560/327637_508188.png)
PNGase F (with His-tag)
$280.00 - $1,100.00
All products have special prices for bulk purchase, please contact for more details if required.
Cat. No.: PNGFH-15k
Cat. No.: PNGFH-75k
Description
PNGase F (Peptide N-Glycosidase F) originates from Elizabethkingia miricola and is an efficient amidase hydrolyzing enzyme. It can cleave high mannose, hybrid, and complex oligosaccharide glycoproteins linked by asparagine. The cleavage site of PNGase F is the amide bond between the inner N-acetylglucosamine (GlcNAc) of the glycoprotein and the asparagine residue, converting the asparagine residue to aspartic acid after enzymatic hydrolysis. This product is expressed via recombinant expression in Escherichia coli, with a His tag, and contains 50% glycerol. It is commonly used for deglycosylation of antibodies and related proteins.
Unit Definition
One enzyme activity unit (U) is defined as the amount of enzyme required to remove more than 95% of carbohydrates from 10 μg of denatured RNase B in a 10 μl reaction system at 37°C for 1 hour.
Inactivation Conditions
Incubation at 75°C for 10 minutes.
Quality Control
- Protein Purity Analysis: Assessed using SDS-PAGE gel electrophoresis, protein purity is not less than 95%.
- Glycosidase and Protease Activity Assay: No detectable endonuclease F1, F2, or F3 activity; no detectable protease activity.
PNGase F Removal
This product carries a His tag and, after reaction, can be removed by affinity chromatography using a different tag from the target glycoprotein.
Storage
Store at -20ºC.
Related:
Only for research and not intended for treatment of humans or animals
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