A modified version of Fusion DNA polymerase obtained by merging the thermostable DNA polymerase of Pyrococcus furiosus (Pfu) and the DNA-binding protein of the thermophilic archaea species Saccharolobus solfataricus (Sso7d). A number of mutations were added to Fusion 2.0 polymerase, increasing the accuracy of the enzyme by approximately 3 times or ~15 times relative to the “native” Taq DNA polymerase

A set of reagents for performing PCR with high-fidelity DNA polymerase. The kit contains individual components such as magnesium ions, a mixture of deoxynucleotide triphosphates (dNTPs) and dimethyl sulfoxide, which allows you to optimize the amplification conditions for the experimenter’s tasks.

Fusion DNA polymerase consists of Pyrococcus furiosus (Pfu) thermostable DNA polymerase and thermophilic archaea DNA-binding protein Sulfolobus solfataricus (Sso7d). The Sso7d protein binds to the minor groove of double-stranded DNA and stabilizes the polymerase-template complex. Due to this, Fusion DNA polymerase has increased processivity, synthesis accuracy, amplification rate, and resistance to PCR inhibitors.

The RNase inhibitor is a 50 kDa recombinant protein expressed in E. coli. It inhibits the ribonuclease activity of eukaryotic enzymes such as RNase A, RNase B, RNase C and protects RNA from non-specific hydrolysis.
The RNase inhibitor is intended for use in applications where the presence of RNases can reduce the quality of experimental results, such as RNA isolation, cDNA synthesis, RT-PCR, transcription and translation in vitro.

The enzyme exhibits high specific activity against double-stranded DNA, while single-stranded DNA or RNA remain intact under standard conditions.

Recombinant Taq DNA polymerase inactivated by thermolabile monoclonal antibodies.

An enzyme derived from the fungus Tritirachium album and produced by expression in the yeast Pichia pastoris. Proteinase K has broad cleavage specificity, cleaves many proteins, and retains its stability in the presence of detergents and urea.

Increasing the proportion of full-length cDNA by removing RNase H-like activity.

The recombinant Taq DNA polymerase has the 5'-3' DNA-dependent polymerase activity and the 5'-3' exonuclease activity of the native Taq DNA polymerase from Thermus aquaticus. The rate of advancement of Taq DNA polymerase depends on the complexity of the DNA template and is approximately 1.5-2 kb/min.

Amplification product obtained using Hot Start Taq DNA polymerase is free from non-specific impurities and primer-dimers.

A large Bacillus stearothermophilus polymerase DNA fragment. The enzyme is highly processive and catalyzes DNA synthesis in the 5'-3' direction.