Fast and robust heat-labile Uracil-N-Glycosylase.
Stable at 25 °C for at least 3 months and at 37 °C 2 weeks.
Heat-labile enzyme (compatible with Sanger sequencing). No reactivation is detected after heat inactivation.
Fast 30-second reaction time.
Tolerant to common inhibitors.
Reaction set-up and shipment without ice.
Glycerol-free formulation is available.
Salini UNG® Uracil-N-Glycosylase is a unique heat-labile enzyme. The protein sequence originates from the bacteria genus Salinivibrio which is frequently found in hypersaline environments. Uracil-N-Glycosylase (UNG) efficiently eliminates uracil from single- or double-stranded DNA by catalyzing the hydrolysis of the N-glycosylic bond and leaving an abasic site. This property is widely used as a part of the PCR carryover contamination prevention strategy. Salini UNG® is a genetically modified enzyme including a Stability TAG - Solis BioDyne’s proprietary and patented polypeptide stabilization technology that makes all our proteins extremely stable at room temperature.
Working concentration: For qPCR application, we recommend using Salini UNG® Uracil-N-Glycosylase at a final concentration of 0.025-0.04 U/μl, for endpoint PCR application at a final concentration of 0.005-0.01 U/μl.
Reaction temperature: If you set up the reaction at room temperature, no additional treatment step is required. If you set up the reaction on ice add the UNG treatment step prior to amplification: 30 seconds at 25 °C. Working temperature 25-40 °C.
Inactivation: 5 min at 70 °C.