Manual

Product Number: RA01

Shipping and Storage

Sealed, dry.

Description

RNase A is an endonuclease that has been well studied and widely used. RNase A hydrolyzes RNA.

Application

1. Drugs: change host cell metabolism, inhibit virus synthesis,
2. Biochemical experiments: Catalyzed RNA degradation, which can specifically hydrolyze the RNA phosphate diester bond hybridized to THE DNA chain, so it can decompose the RNA chain in the RNA/DNA hybrid system.
3. Industrial production，decompose RNA and purify the product.

Specification

1. Source: Bovine (Porcine) pancreas.
2. Appearance: White or pale yellow lyophilized powder.
3. Solvent Transparentness: Not more opalescent than ref.suspensionⅡ.
4. Loss on drying: No more than 5.0%.
5. DNA: Not detectable.
6. Microbial limits: Pseudomonas aeruginosa: Negative; Salmonella: Negative; Staphylococcus aureus: Negative
7. Assay: No less than 50Kunitz units/mg
8. Protein (UV): No less than 65%

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Product Number: RA04

Storage

         Store at -20°C, with a minimum shelf life of 12 months.

Description

         Ribonuclease A, also known as RNase A, is an enzyme that digests RNA and is free of DNase. It is ready to use directly.

         It is used in various common molecular biology, cell biology, and related experiments.

Package

         1ml, 50ml.

Notes

         For your safety and health, please wear a lab coat and disposable gloves when handling.

Related products

•          CL30A, Plasmid Miniprep columns
•          PLC500, ME-tip500, Plasmid Maxi column (Resin)
•          LY03, lysozyme solution
•          PK02, Proteinase K solution

Product Number: RA02

Description

Our Ribonuclease A Solution is a non-specific ribonuclease derived from bovine pancreas that has been modified through protein engineering technology. It is obtained through yeast expression and purification. It does not contain bacterial endotoxins expressed by prokaryotes. Functionally, RNase A is a ribonuclease that can hydrolyze the phosphodiester bond between the 5 ‘- ribose on a nucleoside and the phosphate group on the adjacent pyrimidine nucleoside 3’ – ribose. The resulting 2 ‘, 3’ – cyclic phosphate can be hydrolyzed into the corresponding 3 ‘- nucleoside phosphate. Therefore, single stranded RNA can be specifically degraded at the positions of C and U nucleotide residues. RNase A is very stable. RNase A exhibits high efficacy when acting on single stranded RNA.

This product is widely used to remove RNA contamination from DNA or protein samples.

This product is free from contamination by endonucleases and exonucleases, as well as protease contamination.

Quality Index

Note

For your safety and health, please wear lab clothes and protective gloves when using.

Ribonuclease A (RNase A) is a genetically engineered endonuclease which is originally from bovine genome. The product is produced and purified from yeast cells without contamination of endotoxin.

RNase A is a very stable endoribonuclease and a single chain polypeptide containing four disulfide bridges. Solutions of RNase A have been reported to withstand temperatures up to 100°C. The highest activity is exhibited with single stranded RNA. Activators of RNase A include potassium and sodium salts.

A major application for RNase A is the removal of RNA from preparations of biological products, such as plasmid DNA or protein samples. It is also used in RNA sequence analysis and protection assays.

• CAS No.: 9001-99-4
• E.C.: 3.1.27.5
• Source: Pichia pastoris cells with cloned gene encoding genetically engineered Bovine pancreatic ribonuclease.
• Activity: ≥40 Kunitz units/mg Protein
• Molecular weight: 14.3 kDa
• Form: Lyophilized Powder
• Grade: Molecular biology level
• Purity: ≥ 90%; (SDS-PAGE)
• Endotoxin: None detected (Tachypleus Amebocyte Lysate)
• Foreign activity: Endonuclease and exonuclease, none detected
• NICKase and DNase, none detected
• Optimal pH: 7.6 (activity range of 6-10)
• Optimal temperature: 60°C (activity range of 15-70°C)
• Shelf life: 3 years (-20°C)

Transportation and Storage

Storage temperature: -20°C.

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