TransStart® Taq DNA Polymerase (with 2.5 mM dNTPs)

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Catalog Number:AP141-13

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Description

TransStart® Taq DNA Polymerase is a hot start Taq DNA polymerase containing Taq DNA polymerase and two proprietary DNA binding proteins. At room temperature, one binding protein binds to double-strand DNA template and another binding protein binds to primer. These unique formulations effectively neutralize the DNA polymerase activity at room temperature. Blocking proteins are released from templates and primers during the initial denaturation. This double blocking method has higher efficiency than antibody based, or chemically modified hot start PCR.

  • TransStart® Taq DNA Polymerase offers 18-fold fidelity as compared to EasyTaq® DNA Polymerase.
  • Extension rate is about 1-2 kb/min.
  • Template-independent “A” can be generated at the 3’ end of the PCR product. PCR products can be directly cloned into pEASY®-T vectors.
  • Reduced nonspecific amplification and primer dimer formation.
  • Different from Taq antibody, no risk of contamination from mammalian DNA.
  • Different from chemical modification, long denaturing step is not needed.
  • Amplification of genomic DNA fragment up to 15 kb.

Applications

  • Complex templates
  • GC/AT-rich templates
  • Multiplex PCR
  • High yield PCR

Storage
at -20 ℃ for two years

Shipping
Dry ice (-70 ℃)

Product Composition
Component    AP141-01/11    AP141-02/12     AP141-03/13
TransStart ® Taq DNA Polymerase           250 U×1           500 U×1            500 U×6
10×TransStart ® Taq Buffer               1.2 ml           1.2 ml×2          1.2 ml×12
2.5 mM dNTPs        -/800 μl×1        -/800 μl×2         -/1.2 ml×8
10×GC Enhancer           200 μl×1           400 μl×1               1 ml×1
6×DNA Loading Buffer           500 μl×1              1 ml×1               1 ml×2
References

1 Mi J, Zhou X, Sun R, et al. Disabling spidroin N-terminal homologs’ reverse reaction unveils why its intermolecular disulfide bonds have not evolved for 380 million years[J]. International Journal of Biological Macromolecules, 2023.(IF 8.20)

2 Hao T, Xie Z, Wang M, et al. An anaerobic bacterium host system for heterologous expression of natural product biosynthetic gene clusters[J]. Nature communications, 2019.(IF 10.70)

3 Fan Z, Zhao J, Chai X, et al. A Cooperatively Activatable, DNA‐based Fluorescent Reporter for Imaging of Correlated Enzymatic Activities[J]. Angewandte Chemie International Edition, 2021.(IF 15.33)

4 Chi X, Yan R, Zhang J, et al. A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2[J]. Science, 2020.(IF 41.00)

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