This product is a mouse-derived RNase inhibitor expressed via a recombinant E. coli expression system, with a molecular weight of 50 kDa. It specifically binds to RNase A, B, and C in a 1:1 ratio non-competitively, inhibiting the activity of all three enzymes. This reaction is reversible; the complex can be dissociated using urea or thiol-containing reagents, inactivating the inhibitor and allowing RNase to regain its activity. This product is ineffective against RNase 1, RNase T1, S1 nuclease, RNase H, or RNases derived from Aspergillus species. Furthermore, RNase Inhibitor, Murine exhibits no inhibitory effect on polymerase activity when used with Taq DNA polymerase, AMV or M-MLV reverse transcriptase, or phage RNA polymerases (SP6, T7, or T3). The recombinant RNase Inhibitor, Murine amino acid sequence does not contain cysteine. It has been demonstrated that the cysteine in the human RNase Inhibitor sequence is highly sensitive to oxidation, leading to inhibitor inactivation. Consequently, RNase Inhibitor, Murine exhibits significantly enhanced antioxidant stability compared to human/porcine RNase inhibitors and remains stable at lower DTT concentrations (1 mM). This makes it advantageous in reactions unsuitable for high DTT concentrations, such as RT-PCR. Primary applications include:

• Inhibition of common eukaryotic RNases
• Suitable for cDNA synthesis and RT-PCR
• In vitro transcription and translation
• Enzyme-catalyzed RNA labeling reactions
• Other experiments requiring preserved RNA integrity