TaqDNA Polymerase is a thermostable enzyme that synthesizes DNA from single-stranded templates in the presence of dNTPs and a primer. The enzyme consists of a single polypeptide with a molecular weight of 94 kDa. It has a 5´→3´ DNA polymerase activity and a 5´→3´ exonuclease activity. Recombinant enzyme is purified from the cloned Thermus aquaticus DNA polymerase gene expressed in E. coli.
KlenTaq® is a Klenow-fragment analog of Taq DNA polymerase. It is a 5’-exonuclease deficient Taq polymerase (an N-terminal deletion of Taq) with improved fidelity, robust and thermostability.
KlenTaq-P is a 5’-exonuclease deficient Taq polymerase (an N-terminal deletion of Taq) with improved fidelity and thermostability, plus an extra mutation rendering the enzyme PAP function (Pyrophosphorolysis-activated polymerization). The enzyme is capable of detecting rare mutations, large heterozygous deletions, gene duplications, etc. in the presence of a large excess of wild type allele and inorganic pyrophosphate). In theory PAP can detect a single base mutation in 3x1011copies of wild type allele.
Taq and Klentaq LA® (Long Accurate) versions of the enzymes are mixtures of Taq / KlenTaq and a proof reading enzyme. They can be used to amply a long gene target with high fidelity.