Salini UNG® Uracil-N-Glycosylase

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 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.

• Applications:Widely used to eliminate carryover contamination in PCR and LAMP; Enhancer of cloning efficiency of PCR products; Site-directed mutagenesis; Protein-DNA interaction studies; Glycosylase-mediated single nucleotide polymorphism detection (GMPD); Study of DNA repair and mutation detection; SNP genotyping