Thermostable RNase H
Thermostable RNase H specifically recognizes and cleaves the phosphodiester bonds of an RNA strand in an RNA-DNA hybrid while leaving the DNA strand intact. This thermostable nuclease exhibits the same enzymatic properties as E. coli RNase H, but is active at much higher temperatures.
- Recombinant enzyme supplied with 10X Reaction Buffer
- Does not digest single or double-stranded DNA
- Active and stable above 37°C over a broad temperature range, with activity increasing with temperature
- Requires magnesium chloride for activity
- Inactivated with proteinase K treatment or addition of excess EDTA
Thermostable RNase H is an endoribonuclease that is functional at high temperatures and selectively hydrolyzes the phosphodiester bonds of an RNA strand in an RNA:DNA hybrid molecule, while leaving the DNA strand intact. In addition, Thermostable RNase H does not degrade single- or double-stranded RNA or DNA. While the Thermostable and E. coli RNase H homologs both exhibit these same endoribonucleolytic properties, the thermostable enzyme displays activity at higher temperatures with optimal activity above 65°C. These properties allow use in applications where higher assay temperatures are desired.
Product SourceAn E. coli strain carrying a codon optimized plasmid encoding RNase H from the extreme thermophile Thermus thermophilus.
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