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R5000

Sigma-Aldrich

Ribonuclease A from bovine pancreas

Type II-A, ≥60% (SDS-PAGE), >= 60 Kunitz units/mg protein

Synonym(s):

Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine pancreas

Quality Level

type

Type II-A

form

solid

specific activity

>= 60 Kunitz units/mg protein

mol wt

~13,700

concentration

≥60% (SDS-PAGE)

technique(s)

cell based assay: suitable

impurities

salt, essentially free

suitability

suitable for molecular biology

application(s)

diagnostic assay manufacturing

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.

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 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 hybridase activity of human ribonuclease-1. Ribonuclease A from bovine pancreas has also been used in a study to investigate particle-based and monolithic columns for cation exchange protein displacement chromatography.

Features and Benefits

Our highly stable Ribonuclease A, RNase A, is suitable for removal of RNA, RNA sequencing, and DNA purification.

Preparation Note

Chromatographically purified

Analysis Note

Protein determined by E.
RNase A purity determined by SDS-PAGE

inhibitor

Product No.
Description
Pricing

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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Beata Schmidt et al.
Journal of chromatography. A, 1018(2), 155-167 (2003-11-19)
The overall topic of the investigation was the separation of basic proteins by cation exchange displacement chromatography. For this purpose two principal column morphologies were compared for the separation of ribonuclease A and alpha-chymotrypsinogen, two proteins found in the bovine
Elie Saliba et al.
eLife, 7 (2018-03-24)
The yeast Target of Rapamycin Complex 1 (TORC1) plays a central role in controlling growth. How amino acids and other nutrients stimulate its activity via the Rag/Gtr GTPases remains poorly understood. We here report that the signal triggering Rag/Gtr-dependent TORC1
Nana Asare et al.
Toxicology and applied pharmacology, 230(2), 175-186 (2008-04-18)
Mechanistic studies of nitro-PAHs (polycyclic aromatic hydrocarbons) of interest might help elucidate which chemical characteristics are most important in eliciting toxic effects. 1-Nitropyrene (1-NP) is the predominant nitrated PAH emitted in diesel exhaust. 1-NP-exposed Hepa1c1c7 cells exhibited marked changes in
Stephanie E Siegmund et al.
Human molecular genetics, 26(23), 4588-4605 (2017-10-04)
Mitochondrial disorders affecting oxidative phosphorylation (OxPhos) are caused by mutations in both the nuclear and mitochondrial genomes. One promising candidate for treatment is the drug rapamycin, which has been shown to extend lifespan in multiple animal models, and which was
Nicoletta Potenza et al.
Nucleic acids research, 34(10), 2906-2913 (2006-06-02)
Human ribonuclease-1 (hRNase-1) is an extracellular enzyme found in exocrine pancreas, blood, milk, saliva, urine and seminal plasma, which has been implicated in digestion of dietary RNA and in antiviral host defense. The enzyme is characterized by a high catalytic

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