|25 units/100 μL protein|
|ml wt||Mᵣ = 60 kDa|
|packaging||300 μL vial with lyophilized powder |
|optimum pH||5.0 - 5.5|
|shipped in||shipped at room temperature|
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.
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.
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.
100 μL enzyme solution in 10 mM sodium phosphate were freeze-dried.
Larger quantities for your development, manufacturing or research applications needed?
Please enquire at firstname.lastname@example.org
|Safety Information for this product is unavailable at this time. |
Our team has experience in all areas of research including Life Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact us at email@example.com