Description
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 doublestranded 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 [1].
[1] Kahre, O. et al., Compositions for increasing polypeptide stability and activity, and related methods, EP2501716B1 (2015) and US9321999B2 (2016).
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
