DNaseMe, dsDNase (EN33)DNaseMe is a 42.8 kDa recombinant endonuclease, derived from marine amphipods, expressed in Pichia pastoris. The enzyme displays high specific activity towards double-stranded DNA leaving single-stranded DNA or RNA undamaged in standard conditions. DNaseMe is highly active in a broad spectrum of temperatures, buffer conditions and pH. The specific activity is similar to bovine DNase I however, DNaseMe is characterized by higher stability in demanding reaction and storage conditions (e.g. high salt and detergent containing buffers, elevated temperature). These features make DNaseMe extremely useful for rapid and “RNA safe” degradation of genomic DNA, where absence of ribonucleases is critical to maintain the integrity of RNA.
Saltonase, HL-Nuclease (EN32)Saltonase, (HL-Nuclease) is a cold-active, heat-labile recombinant endonuclease produced in E.coli. Saltonase originates from psychrophilic bacteria and effectively digests all types of DNA and RNA substrates in different buffer conditions and a broad range of temperatures. It is very active in demanding conditions, including low temperatures and environment with high salt content. These features make Saltonase extremely useful for removing undesired nucleic acids contamination during purification of proteins in laboratory and manufacturing workflows.
Masterase, HL-dsDNase (EN31)Masterase, HL-dsDNase is a 43.3 kDa heat-labile recombinant endonuclease, derived from a cold water eukaryotic organism, expressed in Pichia pastoris. The enzyme displays high specific activity towards double-stranded DNA leaving single-stranded DNA or RNA undamaged in standard conditions. Masterase can be easily inactivated by heat treatment in moderate temperatures. It is intended for applications where the presence of dsDNA influences experiments’ results in thermo-sensitive applications and it is extremely useful for rapid and safe purification of RNA or proteins samples from contaminating DNA.
RNase A (RP145)The Ribonuclease A (RNase A) is a 13.7 kDa (monomer) endoribonuclease isolated from bovine pancreas, which selectively cleaves single-stranded RNA 3’ next to pyrimidine residues (cytosine, uracil). It degrades RNA to cyclic nucleotide monophosphates to 5’- OH and 2’-, 3’-cyclic monophosphate. The enzyme exhibits no endonuclease or exonuclease activity towards DNA substrates. The RNase A is used to remove RNA during the isolation procedures of plasmid and genomic DNA.
RNase H (RT34)
RNase H is a 18.9 kDa recombinant endoribonuclease purified from an Escherichia coli strain. The enzyme hydrolyses specifically the phosphodiester bonds of RNA hybridized to DNA and produces 5´ phosphate-terminated oligoribonucleotides and single-stranded DNA. The enzymes does not degrade single and double-stranded DNA or unhybridized RNA. It is a key enzyme in the removal of mRNA after first-strand cDNA synthesis. Treating cDNA with RNase H prior to PCR can improve sensitivity as RNA bonded to the cDNA template may prevent binding of the amplification primers in a PCR reaction. RNase treatment is often necessary when amplifying longer, full-length cDNA targets. In addition, this enzymes is useful for the removal of poly(A) tails on mRNAs after hybridization with oligo(dT) and also for the site-specific enzymatic cleavage of RNA.