Recombinant RNase Inhibitor (Murine, Glycerol-Free)

Recombinant RNase Inhibitor (Murine) is a 50 kDa recombinant protein of murine origin. The inhibitor specifically inhibits RNases A, B and C. It inhibits RNases by binding noncovalently in a 1:1 ratio with high affinity. 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, AMV or M-MuLV Reverse Transcriptases, or Phage RNA Polymerases (SP6, T7, or T3). Recombinant RNase Inhibitor (Murine) does not contain the pair of cysteines identified in the human version that is very sensitive to oxidation, which causes inactivation of the inhibitor. As a result, Recombinant RNase Inhibitor (Murine) has significantly improved resistance to oxidation compared to the human/porcine RNase inhibitors, and is stable at low DTT concentrations (less than 1 mM). This makes it ideal for reactions where high concentration DTT is adverse to the reaction (eg. Real-time RT-PCR). Recombinant RNase Inhibitor (Murine, Glycerol-Free) is a glycerol free formulation of our regular Recombinant RNase Inhibitor (Murine) and is well suited for automated high throughput testing, lyophilization or where accurate pipetting of small volumes are crucial. Recombinant RNase Inhibitor (Murine, Glycerol-Free) is available in different sizes and concentrations.