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R5250

Sigma-Aldrich

Ribonuclease A from bovine pancreas

Type X-A, ≥90% (SDS-PAGE), ≥70 Kunitz units/mg protein

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Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
CAS Number:
9001-99-4
Enzyme Commission number:
3.1.27.5 (BRENDA, IUBMB)
MDL number:
MFCD00132181
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

200

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

Application

Product No.
Description
Pricing

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Downregulation of the long non-coding RNA taurine-upregulated gene 1 inhibits glioma cell proliferation and invasion and promotes apoptosis
Zhao Z, et al.
Oncology Letters, 15(3), 4026-4032 (2018)
Ribonucleases: From Prototypes to Therapeutic Targets
Loverix S and Steyaert J
Current Medicinal Chemistry, 10(9), 779-785 (2003)
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
Free extracellular miRNA functionally targets cells by transfecting exosomes from their companion cells
Bryniarski K, et al.
PLoS ONE, 10(4), e0122991-e0122991 (2015)
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Protocols

Enzymatic Assay of Ribonuclease A (EC 3.1.27.5)

This procedure may be used for determination of Ribonuclease A (RNase A) activity.

Chromatograms

application for HPLC

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