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RNase A, EC:3.1.27.5, DNase free. For the elimination of RNA during plasmid DNA preparation. Select from powder or solution.
RNase A, EC:3.1.27.5, also known as Ribonuclease A, is a type of endonuclease enzyme that specifically cleaves the phosphodiester bonds in RNA molecules. It is a small protein composed of 124 amino acid residues with a molecular weight of about 13.7 kDa. RNase A is highly stable and resistant to proteolysis, heat, and changes in pH. It is found in the pancreas of mammals, where it is secreted into the small intestine to aid in the digestion of RNA molecules from ingested food. RNase A has many applications in molecular biology, including the removal of RNA from DNA samples and the degradation of unwanted RNA in gene expression studies.
- Enzyme name: Ribonuclease A
- Source: Bovine pancreas
- Molecular weight: 13.7 kDa
- Optimal pH: 7.0-8.0
- Optimal temperature: 37°C
- Activity: RNase A specifically cleaves single-stranded RNA at the 3' end of pyrimidine residues (uracil, cytosine)
- Inhibitors: RNase inhibitors such as RNasin and vanadyl ribonucleoside complex (VRC)
- Chemicals that can affect activity: EDTA, urea, guanidine hydrochloride
- Buffer compositions: RNase A is active in a variety of buffers, including Tris-HCl, phosphate, and acetate buffers.
It's worth noting that RNase A is highly stable and resistant to denaturation, which makes it a popular choice for RNA research applications. However, its stability also means that it can be difficult to inactivate or remove from samples, so caution should be taken to prevent RNA degradation during experiments.
Activity: ≥ 50 Kunitz units/mg.
DNase Contamination: Not detected.
Form: Supplied as solution or lyophilized powder.
GenCatch™ Total RNA Miniprep Protocol:
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