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R5500

Sigma-Aldrich

Ribonuclease A from bovine pancreas

Type XII-A, ≥90% (SDS-PAGE), 75-125 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

biological source

bovine pancreas

Quality Level

type

Type XII-A

Assay

≥90% (SDS-PAGE)

form

lyophilized powder

specific activity

75-125 Kunitz units/mg protein

mol wt

~13,700

impurities

salt, essentially free

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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This Item
R5125R4875R5000
assay

≥90% (SDS-PAGE)

assay

≥85% RNase A basis (SDS-PAGE)

assay

-

assay

-

form

lyophilized powder

form

lyophilized powder

form

powder

form

solid

specific activity

75-125 Kunitz units/mg protein

specific activity

85-140 Kunitz units/mg protein

specific activity

≥50 Kunitz units/mg protein

specific activity

>= 60 Kunitz units/mg protein

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

impurities

salt, essentially free

impurities

salt, essentially free

impurities

salt, essentially free

impurities

salt, essentially free

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.

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.

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.

Preparation Note

Salt fractionated and chromatographically purified.

Analysis Note

Protein determined by E.

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Vlad Zabrouskov et al.
Biochemistry, 45(3), 987-992 (2006-01-18)
Although deamidation at asparagine and glutamine has been found in numerous studies of a variety of proteins, in almost all cases the analytical methodology that was used could detect only a single site of deamidation. For the extensively studied case
Amy B Emerman et al.
Methods in molecular biology (Clifton, N.J.), 1413, 303-324 (2016-05-20)
RNAs associate with the mitotic spindle in a variety of organisms, where they can spatially regulate protein production, ensure their proper segregation during cell division, or perform translation-independent roles in spindle formation. The identification of spindle-associated RNAs is an important
Amaya Albalat et al.
Methods in molecular biology (Clifton, N.J.), 984, 153-165 (2013-02-07)
The analysis of proteins and peptides in biological fluids is becoming more important as they are potential sources of diagnostic biomarkers of disease. The complexity of body fluids is such that no single technique can both identify and quantify all
Xin-Miao Fu et al.
Biochimica et biophysica acta, 1814(4), 487-495 (2011-01-18)
Protein disulfide isomerase (PDI) and its pancreatic homolog (PDIp) are folding catalysts for the formation, reduction, and/or isomerization of disulfide bonds in substrate proteins. However, the question as to whether PDI and PDIp can directly attack the native disulfide bonds
Romina Ponzielli et al.
Nucleic acids research, 36(21), e144-e144 (2008-10-23)
High-throughput, microarray-based chromatin immunoprecipitation (ChIP-chip) technology allows in vivo elucidation of transcriptional networks. However this complex is not yet readily accessible, in part because its many parameters have not been systematically evaluated and optimized. We address this gap by systematically

Protocols

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

Chromatograms

application for HPLC

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