R5250
Ribonuclease A from bovine pancreas
Type X-A, ≥90% (SDS-PAGE), ≥70 Kunitz units/mg protein
Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
bovine pancreas
Quality Level
type
Type X-A
assay
≥90% (SDS-PAGE)
form
buffered aqueous solution
specific activity
≥70 Kunitz units/mg protein
mol wt
~13,700
foreign activity
protease, essentially free
storage temp.
−20°C
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)
InChI key
CQOVPNPJLQNMDC-UHFFFAOYSA-N
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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.
Ribonucleases do not hydrolyze DNA, because the DNA lacks 2′-OH groups essential for the formation of cyclic intermediates. RNase can hydrolyze RNA from protein samples. Pancreatic RNase A specifically cleaves at the 3′-side of pyrimidine (uracil or cytosine) phosphate bonds. The ribonuclease (RNase) gene is mapped to human chromosome 14.
Application
- 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.
Ribonuclease A from bovine pancreas has been used to treat human glioblastoma U251 cell line prior to harvesting, for flow cytometry analysis, T suppressor cells and embryonic stem cell chromatin.
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 the mechanism of heavy metal ions on RNase activity. Ribonuclease A from bovine pancreas has also been used in a study to investigate the performance of oligomeric poly(diallyldimethylammonium chloride) as displacer for cation-exchange displacement chromatography of proteins.
Biochem/physiol Actions
The structure of Ribonuclease A (RNase A) comprises of four disulfide and catalytic triad of two histidines crucial for its functionality. RNase A displays three-dimensional domain swapping of the α-helical N-terminal and the C-terminal β-strand. It can exist as dimer or oligomers. The level of RNase is elevated in cancers and infectious diseases. RNase A family of enzymes serve as potential drug targets. The homolog and variants of RNase A are potential chemotherapeutic agents.
Features and Benefits
Our highly stable Ribonuclease A, RNase A, is suitable for removal of RNA, RNA sequencing, and DNA purification.
Physical form
Solution in 0.2 M sodium phosphate buffer, pH 6.4
Preparation Note
A further chromatographic purification of R5503 to yield essentially pure RNAse A
Analysis Note
Protein determined by E.
RNase A purity determined by SDS-PAGE
inhibitor
Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Ribonucleases as Novel Chemotherapeutics
Lee JE and Raines RT
BioDrugs : Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy, 22(1), 53-58 (2008)
Fa-shui Hong et al.
Guang pu xue yu guang pu fen xi = Guang pu, 22(4), 651-654 (2003-08-27)
This paper studied mechanism of Ce3+, Cd2+, Pb2+ on RNase activity from bovine pancreas. The results showed that the activity of RNase was enhanced under the treatment by Ce3+, Cd2+, Pb2+ at lower concentration (10-60 or 10-30 mumol.L-1), but was
Insight into ribonuclease A domain swapping by molecular dynamics unfolding simulations
Esposito L and Daggett V
Biochemistry, 44(9), 3358-3368 (2005)
The crystal structure of ribonuclease A in complex with thymidine-3?-monophosphate provides further insight into ligand binding
Doucet N, et al.
Proteins: Structure, Function, and Bioinformatics, 78(11), 2459-2468 (2010)
B Schmidt et al.
Journal of chromatography. A, 944(1-2), 149-159 (2002-02-08)
A novel type of linear polyelectrolyte, namely poly-DADMAC [poly(diallyldimethylammonium chloride)], was prepared and studied as a displacer for cation-exchange displacement chromatography of proteins. In contrast to the commercially available polymers of that chemistry, the novel type of poly-DADMAC introduced here
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