Salini™ UNG Uracil-N-Glycosylase, 100 U

Product Details

Datasheet

• 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 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.
• 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