Thermo T7 RNA Polymerase (TT7) (Highly concentrated)

Cosmo Bio USA

Thermo T7 RNA Polymerase (TT7) (Highly concentrated)

16

Research Use Only

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: <ol> SDS-polyacrylamide gel analysis for purity Functional absence of exonuclease, endonuclease, and RNase Performance in a transcription reaction at both 37°C and 50°C </ol> References <ol> 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) 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) 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) 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) </ol>

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