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.
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