Recombinant human Ribonuclease A/RNASE 1 protein

RNASE1, also known as ribonuclease A, is a member of pancreatic ribonuclease enzyme family. It is a relatively small protein and is a basic protein (pI = 9.63) . Also, It has four disulfide bonds in its native state. It cleaves specifically after pyrimidine nucleotides. Cleavage takes place in two steps: first, the 3’,5’-phosphodiester bond is cleaved to generate a 2’,3’-cyclic phosphodiester intermediate; second, the cyclic phosphodiester is hydrolyzed to a 3’-monophosphate. (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. It 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. Recombinant human RNASE1, fused to His-tag at C-terminus, was expressed in HEK293 cell and purified by using conventional chromatography techniques.