Taq DNA Polymerase Recombinant Mouse mAb (S-4586)

Taq DNA polymerase is a thermostable DNA-dependent DNA polymerase isolated from the thermophilic bacterium Thermus aquaticus, with a molecular weight of approximately 94 kDa. It has become one of the most influential tool enzymes in molecular biology due to its central role in the polymerase chain reaction (PCR). The enzyme possesses 5′→3′ DNA polymerase activity, which enables it to use single-stranded DNA as a template and oligonucleotide primers as starting points to extend new strands in the 5′→3′ direction according to complementary base pairing, catalyzing the incorporation of deoxynucleotides. It also exhibits 5′→3′ exonuclease activity, allowing it to remove downstream chains during DNA synthesis, a property that makes it suitable for real-time quantitative PCR detection systems such as TaqMan probes. However, Taq polymerase lacks 3′→5′ exonuclease activity (i.e., proofreading function), so its amplification products undergo non-template-dependent addition of an extra deoxyadenosine (A tail) at the 3′ end, a feature exploited in TA cloning. The optimal reaction temperature for Taq polymerase is approximately 72°C, and it remains stable at high temperatures such as 95°C, but its amplification fidelity is relatively low (base misincorporation rate of approximately 2×10⁻⁵ per cycle). Through site-directed mutagenesis to optimize its functions, various derivatives have been developed, including high-fidelity versions (such as proofreading enzymes required for high-throughput sequencing), direct PCR versions that tolerate multiple inhibitors, and rapid versions supporting ultra-fast amplification, greatly advancing life science research and clinical diagnostics.