Recombinant RNase Inhibitor
Recombinant RNase Inhibitor
Brand: Takara Bio.
In stock
SKU
Recombinant RNase Inhibitor
Recombinant RNase Inhibitor forms a 1:1 complex with RNase A and inhibits RNase activity. This reaction is reversible, and ribonuclease activity can be recovered by dissociating the complex with urea or sulfhydryl reagent. This reaction irreversibly inactivates the inhibitor. Recombinant RNase Inhibitor can be added directly to reaction mixtures containing RNA. In addition, because it is a protein, it differs from other competitive inhibitors (nucleotides and inorganic phosphates) by being able to be easily removed from the reaction system using phenol extraction.
Applications
- cDNA synthesis (Ribonuclease Inhibitor: 0.5 U/µl reaction)
- In vitro translation (Ribonuclease Inhibitor: 1 U/µl reaction)
- In vitro transcription using cell-free extract (Ribonuclease Inhibitor: 20 U/µl reaction)
- In vitro transcription with SP6 or T7 RNA Polymerase (Ribonuclease Inhibitor: 1 U/µl reaction)
- Polysome isolation (Ribonuclease Inhibitor: 1,000 U/ml reaction)
Components
2313A: 5,000 U
2313B: 5 x 2313A (25,000 U)
Source
E. coli containing a plasmid that carries the porcine RNase Inhibitor gene
Storage
–20°C
Concentration
40 U/µl
Blackburn, P. Ribonuclease inhibitor from human placenta: rapid purification and assay. J. Biol. Chem. 254, 12484–7 (1979).
Blackburn, P., Wilson, G. & Moore, S. Ribonuclease inhibitor from human placenta. Purification and properties. J. Biol. Chem. 252, 5904–10 (1977).
Burton, L. E. & Fucci, N. P. Ribonuclease inhibitors from the livers of five mammalian species. Int. J. Pept. Protein Res. 19, 372–9 (1982).
Eichler, D. C., Tatar, T. F. & Lasater, L. S. Effect of human placental ribonuclease inhibitor in cell-free ribosomal RNA synthesis. Biochem. Biophys. Res. Commun. 101, 396–403 (1981).
Martynoff, G. de, Pays, E. & Vassart, G. Synthesis of a full-length DNA complementary to thyroglobulin 33 S messenger RNA. Biochem. Biophys. Res. Commun. 93, 645–653 (1980).
Scheele, G. & Blackburn, P. Role of mammalian RNase inhibitor in cell-free protein synthesis. Proc. Natl. Acad. Sci. U. S. A. 76, 4898–902 (1979).
Turner, P. M., Lerea, K. M. & Kull, F. J. The ribonuclease inhibitors from porcine thyroid and liver are slow, tight-binding inhibitors of bovine pancreatic ribonuclease A. Biochem. Biophys. Res. Commun. 114, 1154–60 (1983).
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