Overview:

Murine RNase inhibitor inhibits RNases by binding noncovalently in a 1:1 ratio with high affinity. The inhibitor has been shown to inactivate a variety of RNases that are present in many tissues and cell types. It is not effective against RNase 1, RNase T1, S1 Nuclease, RNase H or RNase from Aspergillus. In addition, no inhibition of polymerase activity is observed when RNase inhibitor is used with Taq DNA polymerase or M-MLV Reverse Transcriptase. Compared with the human origin RNase inhibitor, the Murine RNases inhibitor doesn’t contain the two Cys residues that are sensitive to oxidation. Therefore, it has improved resistance to oxidant activity and is more ideal for high-DTT-sensitive experiments (e.g. qPCR).

Formulation:

Recombinant protein stored in 20 mM HEPES-KOH pH 7.6, 50 mM KCl, 8 mM DTT, 50% Glycerol

References:

1. Haigis M C, et al: Evolution of ribonuclease inhibitor by exon duplication. Mol Biol Evol. 2002, 19:959-963.
2. Lomax J E, et al: Functional evolution of ribonuclease inhibitor: insights from birds and reptiles. J. Mol Biol. 2014, 126(17): 3041-3056.
3. Dickson K A, et al: Ribonuclease inhibitor: Structure and function. Prog Nucleic Acid Res Mol Biol. 200580:349-374, 2005.