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PNGase H from Terriglobus roseus

Enzyme Commission (EC) Number  ( BRENDA | IUBMB )
Price and Availability
formlyophilized powder
specific activity
25 units/100 μL protein
ml wtM = 60 kDa
Manufacturerqlyco Ltd.
packaging300 μL vial with lyophilized powder
optimum pH5.0 - 5.5
shipped inshipped at room temperature
Pack Size
1 vial
>10 left in stock
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Bulk Ordering and Pricing:
PNGase H+ (Peptide-N-glycosidase H+) can be used for the deglycosylation of glycoproteins. It occurs in the culture fluid of the soil bacterium Terriglobus roseus. 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 H+. The oligosaccharides can be high mannose, hybrid, or complex type. Furthermore, N-glycans with fucose linked (1-3) to the Asn-bound N-acetylglucosamine are also released by PNGase H+, whereas other bacterial Peptide-N-glycosidases such PNGase F cannot release N-glycans bearing this modification.
General description
Glycopetidase H+
Other Notes
For life science research only. Not for use in diagnostic procedures.
Preparation Note
Working concentration:
Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.
Hydrolyzes an N4-(acetyl-β-D-glycosaminyl)asparagine in which the N-acetyl-D-glucosamine residue may be further glycosylated, yielding a (substituted) N-acetyl-β-D-glucoaminylamine and the peptide containing an aspartic residue.
Physical form
100 μL enzyme solution in 10 mM sodium phosphate were freeze-dried.

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Safety Information

Safety Information for this product is unavailable at this time.
Datasheet PNGase H+


Technical Service
Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+  (link to JOVE article)
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