Thermo T7 RNA Polymerase (TT7) (Highly concentrated)

Cosmo Bio LTD

Catalog No: TYB-TRL-252

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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)