Thermo T7 RNA Polymerase (TT7) (Highly concentrated)

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SKU:
TYB-TRL-252
Availability:
Y
1,345$
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Description

Thermo T7 RNA Polymerase (TT7) (Highly concentrated) is 50,000 units of an E. coli-produced, genetically modified T7 RNA polymerase offered at 50U/ul (with 10X reaction buffer). It features an ~85 minute half-life at its optimal reaction temperature of ~50ºC.

Features

  • Exhibits greater specific activity than WT-enzyme at 37-50°C.

Applications

  • RNA probe preparation
  • RNA synthesis for in vitro translation
  • RNA synthesis for RNA splicing studies
  • Capped mRNA synthesis using a cap analogue

Source

  • E. coli strain that carries the genetically modified T7 RNA polymerase gene from T7 phage

10X Reaction buffer (included)

  • 400 mM Tris-HCl (pH 8.0), 500 mM NaCl, 80 mM MgCl2, 50 mM DTT

Storage buffer

  • 20 mM KPO4 (pH 7.7), 100 mM NaCl, 0.1 mM EDTA, 5 mM DTT, 0.01% Triton X-100, 50% Glycerol

Storage

  • -20°C

Quality control assays

This product has passed the following quality control assays:

  1. SDS-polyacrylamide gel analysis for purity
  2. Functional absence of exonuclease, endonuclease, and RNase
  3. Performance in a transcription reaction at both 37°C and 50°C

References

  1. K. Ishikawa, M. Watanabe, T. Kuroita, I. Uchiyama, J.M. Bujnicki, B. Kawakami, M. Tanokura, I. Kobayashi, Discovery of a novel restriction endonuclease by genome comparison and application of a wheat-germ-based cell-free translation assay: PabI (5'-GTA/C) from the hyperthermophilic archaeon Pyrococcus abyssi. Nucleic Acids Res. 3: e112 (2005)
  2. M. Itoh, I. Haga, Q.H. Li, J.Fujisawa, Identification of cellular mRNA targets for RNA-binding protein Sam68. Nucleic Acids Res. 30: 5452-64 (2002)
  3. M. Chamberlin and J. Ring. Characterization of T7-specific ribonucleic acid polymerase. 1. General properties of the enzymatic reaction and the template specificity of the enzyme. J Biol Chem. 248: 2235-44 (1973)
  4. M. Chamberlin and J. Ring. Characterization of T7-specific ribonucleic acid polymerase. II. Inhibitors of the enzyme and their application to the study of the enzymatic reaction. J Biol Chem. 248: 2245-50 (1973)
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