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Ribonuclease A (RNase A), commonly abbreviated as RNase A, is a single-stranded peptide containing four disulfide bonds with a molecular weight of approximately 13.7 kDa. As an endoribonuclease, RNase A specifically degrades cytidine (C) or uridine (U) residues on single-stranded RNA. Specifically, it cleaves the phosphodiester bond formed between the 5’-ribose of one nucleotide and the adjacent pyrimidine nucleotide's 3’-ribose, resulting in the hydrolysis of 2’, 3’-cyclic phosphate into the corresponding 3’-nucleotide phosphate (e.g., pG-pG-pC-pA-pG is cleaved by RNase A to yield pG-pG-pCp and A-PG).

RNase A exhibits its highest activity in cleaving single-stranded RNA and is active under various reaction conditions: at low salt concentrations (0-100mM NaCl), it can cleave single-stranded RNA, double-stranded RNA, and RNA chains formed by RNA-DNA hybrids. However, at high salt concentrations (≥0.3M), RNase A specifically cleaves single-stranded RNA.

The most common application of Ribonuclease A (RNase A) is in the removal of RNA during plasmid DNA or genomic DNA preparation processes. Therefore, the presence of DNase enzyme activity during the preparation process is one of the contaminants that needs attention, and traditional methods such as boiling water bath can be used to inactivate DNase activity. This product does not contain DNase and proteases, and no heat treatment is required before use. Additionally, this product can also be used in molecular biology experiments such as RNA protection analysis and RNA sequencing analysis.

This product is provided in solution form with a concentration of 100 mg/ml. The recommended working concentration ranges from 1-100 μg/ml, depending on the specific application.