RNase A (Ribonuclease A)

Description:

RNase A is a ribonuclease (endonuclease) derived from bovine pancreas that selectively cleaves phosphodiester bonds in RNA at the 3′ end of pyrimidine residues (cytosine and uracil). The enzyme consists of 124 amino acids (molecular weight 13.7 kDa) and has an optimal pH of 7.0–8.0.

Cleavage specificity depends on salt concentration:
At low NaCl concentrations (<0.1 M), RNase A cleaves both single-stranded and double-stranded RNA as well as RNA/DNA hybrids.
At higher NaCl concentrations (>0.3 M), it cleaves only single-stranded RNA.

The enzyme is highly stable and resistant to denaturation or degradation. It can be inhibited by specific RNase inhibitors or certain chemicals (e.g., DEPC, GITC, SDS).

Due to its targeted cleavage, RNase A generates predictable RNA fragments, as shown in the image below, allowing efficient RNA removal or analysis of RNA structure in biological samples.

Specifications:

• Concentration: 10 mg/ml

• Source: Bovine pancreas
• Molecular weight: 13.7 kDa
• Shipping: Room temperature; store at -20 °C upon receipt
• Storage: -20 °C, stable for up to 12 months
• Storage buffer: 50 mM Tris-HCl (pH 7.5), 50% glycerol
• Optimal pH: 7.0–8.0
• Optimal temperature: 37 °C
• Activity: ≥ 50 Kunitz units/mg
• DNase contamination: Not detected

• Protease contamination: Not detected

Applications:

• RNA removal during genomic and plasmid DNA isolation

• RNA elimination from proteins during purification

• Degradation of unwanted RNA in gene expression analysis

• Ribonuclease (RNase) assays and applications

Inhibition and inactivation:

Inhibitors include RNase inhibitors, guanidinium thiocyanate (GITC), diethyl pyrocarbonate (DEPC), sodium dodecyl sulfate (SDS), vanadyl ribonucleoside complex (VRC), 5′-diphosphoadenosine-3′-phosphate (ppA-3′-p), 5′-diphosphoadenosine-2′-phosphate (ppA-2′-p), and heavy metals. RNase A can be inactivated by phenol/chloroform extraction.

Product sizes:

• 1 ml (Cat. No. 40106S)

• 5 ml (Cat. No. 40106L)