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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:
Enzyme Commission number:
MDL number:
NACRES:
NA.54

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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1 of 4

This Item
R5500R5000R5503
Ribonuclease A from bovine pancreas Type X-A, ≥90% (SDS-PAGE), ≥70 Kunitz units/mg protein

R5250

Ribonuclease A from bovine pancreas

Ribonuclease A from bovine pancreas Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein

R5500

Ribonuclease A from bovine pancreas

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

R5000

Ribonuclease A from bovine pancreas

Ribonuclease A from bovine pancreas Type I-AS, 50-100 Kunitz units/mg protein

R5503

Ribonuclease A from bovine pancreas

specific activity

≥70 Kunitz units/mg protein

specific activity

75-125 Kunitz units/mg protein

specific activity

>= 60 Kunitz units/mg protein

specific activity

50-100 Kunitz units/mg protein

assay

≥90% (SDS-PAGE)

assay

≥90% (SDS-PAGE)

assay

-

assay

-

form

buffered aqueous solution

form

lyophilized powder

form

solid

form

lyophilized powder

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

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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Customers Also Viewed

Ribonucleases as Novel Chemotherapeutics
Lee JE and Raines RT
BioDrugs : Clinical Immunotherapeutics, Biopharmaceuticals and Gene Therapy, 22(1), 53-58 (2008)
Insight into ribonuclease A domain swapping by molecular dynamics unfolding simulations
Esposito L and Daggett V
Biochemistry, 44(9), 3358-3368 (2005)
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
Free extracellular miRNA functionally targets cells by transfecting exosomes from their companion cells
Bryniarski K, et al.
PLoS ONE, 10(4), e0122991-e0122991 (2015)
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)

Protocols

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

Chromatograms

application for HPLC

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