RNase A, Ribonuclease A, is an endoribonuclease that cleaves the phosphodiester bonds of single strand RNA after pyrimidine nucleotides. It attacks at the 3′ phosphate end (For example pG-pG-pC-pA-pG will be cleaved to give pG-pG-pCp and A-pG). The highest activity is exhibited with single stranded RNA. RNase A is a single chain polypeptide containing 4 disulfide bridges. In contrast to RNase B, it is not a glycoprotein. Ribonucleases do not hydrolyze DNA, because the DNA lacks 2′-OH groups essential for the formation of cyclic intermediates. RNase A can also hydrolyze RNA from protein samples. RNase A can be inhibited by alkylation of His12 and His119 and activated by potassium and sodium salts. RNAse is inhibited in the presence of heavy metal ions. RNase is also inhibited competitively by DNA.

Ribonucleases do not hydrolyze DNA, because the DNA lacks 2′-OH groups essential for the formation of cyclic intermediates. RNase can hydrolyze RNA from protein samples. Pancreatic RNase A specifically cleaves at the 3′-side of pyrimidine (uracil or cytosine) phosphate bonds. The ribonuclease (RNase) gene is mapped to human chromosome 14.

Ribonuclease A from bovine pancreas has been used to treat human glioblastoma U251 cell line prior to harvesting, for flow cytometry analysis, T suppressor cells and embryonic stem cell chromatin.

Ribonuclease A is used to remove RNA from DNA plasmid preparations and protein samples. Ribonuclease A is used for RNase protection assays, to remove unspecifically bound RNA, analysis of RNA sequences, to hydrolyze RNA contained in protein samples, and the purification of DNA. Ribonuclease A from bovine pancreas has been used in a study to assess the mechanism of heavy metal ions on RNase activity. Ribonuclease A from bovine pancreas has also been used in a study to investigate the performance of oligomeric poly(diallyldimethylammonium chloride) as displacer for cation-exchange displacement chromatography of proteins.

The structure of Ribonuclease A (RNase A) comprises of four disulfide and catalytic triad of two histidines crucial for its functionality. RNase A displays three-dimensional domain swapping of the α-helical N-terminal and the C-terminal β-strand. It can exist as dimer or oligomers. The level of RNase is elevated in cancers and infectious diseases. RNase A family of enzymes serve as potential drug targets. The homolog and variants of RNase A are potential chemotherapeutic agents.

Our highly stable Ribonuclease A, RNase A, is suitable for removal of RNA, RNA sequencing, and DNA purification.

Solution in 0.2 M sodium phosphate buffer, pH 6.4

A further chromatographic purification of R5503 to yield essentially pure RNAse A

Protein determined by E.

RNase A purity determined by SDS-PAGE