Ribonuclease A (RNase A) is a non-specific endoribonuclease derived from bovine pancreas, engineered using protein engineering technology and produced via yeast expression and purification. It is free of bacterial endotoxins commonly associated with prokaryotic expression systems. Functionally, RNase A is an endoribonuclease that hydrolyzes the phosphodiester bond between the 5′-ribose of a nucleotide and the 3′-ribose phosphate of an adjacent pyrimidine nucleotide (cytidine or uridine). This reaction generates a 2′,3′-cyclic phosphate intermediate, which is subsequently hydrolyzed to the corresponding 3′-nucleotide phosphate. Thus, RNase A specifically cleaves single-stranded RNA after C and U residues. RNase A is highly stable and exhibits strong activity against single-stranded RNA. This product is widely used to remove RNA contamination from DNA or protein samples. It is free of endonucleases, exonucleases, and proteases. Features Residue-Free: No residual DNA, RNA, DNase, or protease contamination Animal-Origin Free: RNase A is produced by recombinant expression, with no animal-derived components Precise and Efficient RNA Digestion: Specifically cleaves single-stranded RNA; widely used to remove RNA from DNA or protein preparations Eukaryotic Expression System: Expressed and purified from yeast, free of bacterial endotoxins associated with prokaryotic expression High Stability: RNase A is highly stable under a wide range of conditions Application Removal of RNA from DNA preparations Removal of RNA from protein samples Sample preparation for PCR, cloning, and sequencing General molecular biology workflows requiring RNA digestion Specifications CAS No. 9001-99-4 EC Number 3.1.27.5 Source Recombinant yeast Molecular Weight 14.3 kDa Dilution Buffer 10 mM Tris-HCl (pH 8.0), 20 mM MgCl₂ Storage Buffer 10 mM Tris-HCl (pH 8.0), 20 mM MgCl₂, 50% glycerol Appearance Light yellow, clear solution Stock concentration 10 mg/mL Electrophoretic Purity ≥90% (by SDS-PAGE) Enzyme Activity ≥350 KU/mL DNA/RNA Residue None DNase Contamination None Protease Contamination
