Ribonuclease A, Bovine Pancreas (RNase A)
|Cloning||Storage: -20°CShipping: RT|
Ribonuclease A is used to isolate DNA for RNA-free DNA. Ribonuclease A hydrolyzes RNA at C and U residues, cleaving between the 3’-Phosphate group of a pyrimidine nucleotide and the 5’-hydroxyl group of the adjacent nucleotide, i.e., those cleaving cyclic 2',3'-pyrimidine nucleotide residues either singly or at the termination of purine nucleotide chains (Volkin and Cohn 1953). The composition and structure of ribonuclease A has been extensively investigated. The tertiary structure was reported by Kartha, et al. (1967) and Lin, (1970). Wang, et al. (1975) indicate that flexibility in a three-dimensional structure is essential for optimal catalytic activity. Ribonuclease is inhibited by heavy metal ions and is competitively inhibited by DNA. The effect of denatured DNA is much greater than that of the native nucleic acid (Sekine et al. 1969).
60u/mg protein (Assayed by Kunitz method)
One unit will cause the hydrolysis of RNA at that rate where the velocity constant k equals unity (Kunitz units) at 25ºC and pH 5.0.
DNase: ( 1.5mg/ml): None Detected
Protease: None Detected
Soluble at 10mg/ml in analytical grade water. Colorless, clear, complete.
E.C.22.214.171.124; Ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; Ribonuclease 1
Storage and Stability:
Best stored desiccated at -20°C or below. Stable for 12 months. However, the enzyme is stable for years stored as a refrigerated dry powder or frozen in aqueous solution.
Source: Bovine pancreas
Purity: Purified by ion exchange chromotography (~ 95%).
Form: Supplied as a white to off-white powder
Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
US Biological application reference: Cheng, C.-C. et al., (2009) J. Cell Science 122:4473-4480. 1. Kunitz, J. Biol. Chem. 164: 563 (1946). 2. Hirs, et al., J. Biol. Chem. 200: 493 (1953). 3. Kalnitsky, G., Hummel, J.P., Dierks, C., J. Biol. Chem. 234: 1512 (1959).