R5125
Ribonuclease A from bovine pancreas
Type III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein
Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
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About This Item
CAS Number:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
232-646-6
MDL number:
Specific activity:
85-140 Kunitz units/mg protein
Assay:
≥85% RNase A basis (SDS-PAGE)
Biological source:
bovine pancreas
SMILES string
[nH]1cnc(c1)CC(NC(=O)CCN)C(=O)O
InChI key
CQOVPNPJLQNMDC-UHFFFAOYSA-N
InChI
1S/C9H14N4O3/c10-2-1-8(14)13-7(9(15)16)3-6-4-11-5-12-6/h4-5,7H,1-3,10H2,(H,11,12)(H,13,14)(H,15,16)
biological source
bovine pancreas
type
Type III-A
assay
≥85% RNase A basis (SDS-PAGE)
form
lyophilized powder
specific activity
85-140 Kunitz units/mg protein
mol wt
~13,700
technique(s)
cell based assay: suitable
impurities
salt, essentially free
suitability
suitable for molecular biology
application(s)
diagnostic assay manufacturing
foreign activity
protease, essentially free
storage temp.
−20°C
Quality Level
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Related Categories
Application
Ribonuclease A is used to remove RNA from DNA plasmid preparations and protein samples. Ribonuclease A is used for RNase protection assays, to remove unspecifically bound RNA, analysis of RNA sequences, to hydrolyze RNA contained in protein samples, and the purification of DNA. Ribonuclease A from bovine pancreas has been used in a study to assess nickel-dependent oxidative cross-linking of a protein. Ribonuclease A from bovine pancreas has also been used in a study to investigate equilibrium constants for nonspecific binding of proteins to DNA.
- RNase A is used to remove RNA from DNA plasmid and genomic DNA preparations and protein samples.
- RNase A is also used in RNA sequence analysis and protection assays.
- RNase A has been used as a tool for computer-aided drug design.
- RNase A supports the analysis of RNA sequences.
- RNase A hydrolyze RNA contained in protein samples.
- Purification of DNA is supported by RNase A.
Biochem/physiol Actions
Ribonuclease A is an endoribonuclease that cleaves single stranded RNA after pyrimidine nucleotides. It attacks at the 3′ phosphate end. Ribonucleases do not hydrolyze DNA, because the DNA lacks 2′-OH groups essential for the formation of cyclic intermediates. RNase can also hydrolyze RNA from protein samples. RNase A can be inhibited by alkylation of His12 and His119 and activated by potassium and sodium salts.
Features and Benefits
Our highly stable Ribonuclease A, RNase A, is suitable for removal of RNA, RNA sequencing, and DNA purification.
Analysis Note
Protein determined by E.
General description
RNase A, Ribonuclease A, is an endoribonuclease that cleaves the phosphodiester bonds of single strand RNA after pyrimidine nucleotides. It attacks at the 3′ phosphate end (For example pG-pG-pC-pA-pG will be cleaved to give pG-pG-pCp and A-pG). The highest activity is exhibited with single stranded RNA. RNase A is a single chain polypeptide containing 4 disulfide bridges. In contrast to RNase B, it is not a glycoprotein. Ribonucleases do not hydrolyze DNA, because the DNA lacks 2′-OH groups essential for the formation of cyclic intermediates. RNase A can also hydrolyze RNA from protein samples. RNase A can be inhibited by alkylation of His12 and His119 and activated by potassium and sodium salts. RNAse is inhibited in the presence of heavy metal ions. RNase is also inhibited competitively by DNA.
Preparation Note
Salt fractionated and chromatographically purified.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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J Yu et al.
Cytometry, 14(4), 428-432 (1993-01-01)
DNA content by flow cytometry was assessed in 47 cases from a series of 130 patients with non-small cell lung carcinoma (NSCLC) given radiation therapy postoperatively. This was done in an attempt to identify which patients might benefit, or not
G Gill et al.
Chemical research in toxicology, 10(3), 302-309 (1997-03-01)
A model protein, ribonuclease A (bovine pancreas), was examined for its ability to coordinate Ni2+ and promote selective oxidation. In the presence of a peracid such as monopersulfate, HSO5-, nickel induced the monomeric RNase A to form dimers, trimers, tetramers
S B delCardayré et al.
Protein engineering, 8(3), 261-273 (1995-03-01)
Bovine pancreatic ribonuclease A (RNase A) has been the object of much landmark work in biological chemistry. Yet the application of the techniques of protein engineering to RNase A has been limited by problems inherent in the isolation and heterologous
Ricardo C de Abreu et al.
Journal of extracellular vesicles, 10(10), e12111-e12111 (2021-08-12)
Small extracellular vesicles (sEVs), through their natural ability to interact with biological membranes and exploit endogenous processing pathways to convey biological information, are quintessential for the delivery of therapeutically relevant compounds, such as microRNAs (miRNAs) and proteins. Here, we used
E S Jenuwine et al.
Analytical biochemistry, 242(2), 228-233 (1996-11-15)
Quantitative zonal DNA affinity chromatography may be used to determine accurate equilibrium constants for the binding of proteins nonspecifically to DNA. Zonal quantitative affinity chromatography has not previously been applied to the determination of binding constants of proteins to DNA
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Global Trade Item Number
| SKU | GTIN |
|---|---|
| R5125-1G | 04061836695514 |
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