Recombinant RNase A is a Cow Full Length protein, expressed in Yeast and with >=90% purity. The predicted molecular weight of the ab300192 recombinant protein is 13.7 kDa.
- Save time and ensure accurate results - use our recombinant Ribonuclease A (RNase A) enzyme to inactivate RNA
- Free from DNA contamination
- Optimal protein bioactivity, stability and reproducibility
- Available in different sizes to fit your experimental needs
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
RNS1, RNASE1, Ribonuclease pancreatic, RNase 1, RNase A
Recombinant RNase A is a Cow Full Length protein, expressed in Yeast and with >=90% purity. The predicted molecular weight of the ab300192 recombinant protein is 13.7 kDa.
- Save time and ensure accurate results - use our recombinant Ribonuclease A (RNase A) enzyme to inactivate RNA
- Free from DNA contamination
- Optimal protein bioactivity, stability and reproducibility
- Available in different sizes to fit your experimental needs
A Kunitz unit of enzyme causes an increase in A300 equivalent to the complete hydrolysis of a 0.05% (w/v) yeast RNA to oligonucleotides in one minute at 25°C and pH 5.0.
Constituents: 90% Ribonuclease, 8% Sucrose
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
Belongs to the pancreatic ribonuclease family.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Ensure the validity of your result using our recombinant RNase A protein ab300192 to remove RNA contaminants that could interfere with protein or enzyme activity assays.
The bioactive ab300192 enzyme is ideal for applications such as RNA preparation and analysis.
Recommended concentration of RNase A ab300192 is 1 to 100 µg/mL depending on the application.
Extinction Coefficient (ε)1% at 280 nm = 7.1
Function
RNase A (previously sold as Biovision's M1517) is an endoribonuclease that specifically cleaves RNA at the phosphodiester bond between the 3’ phosphate group of a pyrimidine nucleotide and 5’-ribose of an adjacent nucleotide.
The highest activity is demonstrated with single stranded RNA. The recombinant enzyme is identical to the native RNase A in amino acid sequence, structure and specifications.
At low salt concentrations (0 to 100 mM NaCl), RNase A cleaves single-stranded and double-stranded RNA as well the RNA strand in RNA-DNA hybrids. However, at NaCl concentrations of 0.3 M or higher, RNase A specifically cleaves single-stranded RNA.
Precipitation may occur at high concentrations (>10 mg/mL) of the enzyme and RNase A has a high affinity to glass surfaces.
The enzyme is inhibited by diethyl pyrocarbonate (DEPC), guanidinium salts, β-mercaptoethanol, heavy metals and RNase-inhibitors.
In order to remove the enzyme from a sample, perform a separation with spin columns or several phenol/chloroform extractions.
Special care and precautions should be taken in the lab with this enzyme to ensure cross contamination with RNA work does not occur.
Ribonuclease A also known as RNase A is a type of ribonuclease enzyme known for its ability to cleave RNA molecules. This enzyme specifically catalyzes the endonucleolytic cleavage of RNA to produce 3'-phosphates and 3'-phosphooligonucleotides terminated by cytidine or uridine. RNase A has a molecular mass of approximately 13.7 kDa and is primarily found in the pancreas of bovines. This protein plays a significant role in RNA metabolism and is often utilized in laboratory research for this purpose.
Ribonuclease A plays an important role in RNA processing and degradation contributing to the regulation of cellular RNA levels. This enzyme does not operate as part of a larger complex but acts independently to degrade single-stranded RNA. The function of RNase A is essential for maintaining cellular homeostasis by controlling the quantity and quality of the cellular RNA ensuring proper turnover and preventing the accumulation of defective or unnecessary RNA molecules.
Ribonuclease A is involved in the RNA degradation pathway which is critical for normal cellular function and gene expression regulation. It collaborates with other nucleases to ensure efficient RNA turnover. RNase A is closely related to proteins like RNase 1 and RNase 5 which also participate in RNA metabolism. Participation of RNase A in this pathway highlights its importance in the regulation of genetic information flow from DNA to RNA.
The malfunction or dysregulation of Ribonuclease A can impact diseases such as cancer and cystic fibrosis. In cancer aberrant RNase A activity can influence RNA levels contributing to unchecked cell proliferation. Moreover RNase A is connected to the inflammation seen in cystic fibrosis via its impact on RNA turnover and immune system signaling. RNase A interactions with proteins such as angiogenin which displays similar enzymatic properties further exemplify its involvement in disease-related pathways.
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