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R5000

Sigma-Aldrich

Ribonuclease A from bovine pancreas

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

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Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

type

Type II-A

form

solid

specific activity

>= 60 Kunitz units/mg protein

mol wt

~13,700

concentration

≥60% (SDS-PAGE)

impurities

salt, essentially free

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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1 of 4

This Item
R4875R5500R6513
vibrant-m

R5000

Ribonuclease A from bovine pancreas

vibrant-m

R4875

Ribonuclease A from bovine pancreas

vibrant-m

R5500

Ribonuclease A from bovine pancreas

vibrant-m

R6513

Ribonuclease A from bovine pancreas

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

-

form

solid

form

powder

form

lyophilized powder

form

lyophilized

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

mol wt

13.7 kDa, ~13,700

concentration

≥60% (SDS-PAGE)

concentration

≥60% (RNase A, SDS-PAGE)

concentration

-

concentration

-

Quality Level

300

Quality Level

300

Quality Level

300

Quality Level

300

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)


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Customers Also Viewed

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
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
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
Zehan Hu et al.
Cell reports, 28(13), 3486-3496 (2019-09-26)
The target of rapamycin complex 1 (TORC1) is a master regulator of cell homeostasis, which promotes anabolic reactions and synchronously inhibits catabolic processes such as autophagy-mediated protein degradation. Its prime autophagy target is Atg13, a subunit of the Atg1 kinase

Protocols

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

Chromatograms

application for HPLC

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