|25 units/100 μL protein|
|ml wt||Mᵣ = 62 kDa|
|packaging||300 μL of buffered aqueous solution|
|optimum pH||5.0 - 5.5|
|shipped in||sent at 4°C|
PNGase F (Peptide-N-glycosidase F is one of the most widely used enzymes for the deglycosylation of glycoproteins. It occurs in the culture fluid of the pathogenic microorganism Elizabethkingia meningosepticum. The enzyme releases asparagine-linked oligosaccharides from glycoproteins and glycopeptides by hydrolyzing the amide of the asparagine (Asn) side chain. A tripeptide with the oligosaccharide-linked asparagine as the central residue is the minimal substrate for PNGase F. The oligosaccharides can be high mannose, hybrid, or complex type. However, N-glycans with fucose linked alpha(1-3) to the Asn-bound N-acetylglucosamine are resistant to the action of PNGase F.
N-Glycosidase F, Peptide N-glycosidase
For life science research only. Not for use in diagnostic procedures.
Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.
Cleaves an entire glycan from a glycoprotein provided the glycosylated asparagine moiety is substituted on its amino and carboxyl terminus with a polypeptide chain.
300 μL enzyme solution.
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|Safety Information for this product is unavailable at this time. |
|No protocol yet available|
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