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R5503

Sigma-Aldrich

Ribonuclease A from bovine pancreas

Type I-AS, 50-100 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 I-AS

form

lyophilized powder

specific activity

50-100 Kunitz units/mg protein

mol wt

~13,700

technique(s)

cell based assay: suitable

impurities

salt, essentially free

suitability

suitable for mRNA or total RNA extracted from cells and tissues

application(s)

diagnostic assay manufacturing

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
R5000R5125R5500
Ribonuclease A from bovine pancreas Type I-AS, 50-100 Kunitz units/mg protein

R5503

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 III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein

R5125

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

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

form

lyophilized powder

form

solid

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

mol wt

~13,700

Quality Level

300

Quality Level

-

Quality Level

-

Quality Level

-

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

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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M P Sasso et al.
Gene, 227(2), 205-212 (1999-02-19)
Molecular evolutionary analyses of mammalian ribonucleases have shown that gene duplication events giving three paralogous genes occurred in ruminant ancestors. The enzymes of the bovine species encoded by these genes, isolated from pancreas, brain and seminal vesicles, present similar enzymological
P Klappa et al.
European journal of biochemistry, 254(1), 63-69 (1998-07-04)
Using a cross-linking approach, we have demonstrated that radiolabeled model peptides or misfolded proteins specifically interact in vitro with two different luminal proteins in a crude extract from sheep pancreas microsomes. One of the proteins was identified as protein disulphide-isomerase
J J Beintema et al.
Cellular and molecular life sciences : CMLS, 54(8), 825-832 (1998-10-07)
Enzymic properties of members of the ribonuclease A superfamily, like the activity on RNA, the preference for either cytosine or uracil in the primary binding site B1, the preference for the other side of the cleaved phosphodiester bond, the B2
Gertrud Forika et al.
International journal of molecular sciences, 21(14) (2020-07-28)
The poor outcome of pancreas ductal adenocarcinomas (PDAC) is frequently linked to therapy resistance. Modulated electro-hyperthermia (mEHT) generated by 13.56 MHz capacitive radiofrequency can induce direct tumor damage and promote chemo- and radiotherapy. Here, we tested the effect of mEHT
Yanchang Li et al.
Molecular cell, 76(1), 126-137 (2019-08-25)
A surprising complexity of ubiquitin signaling has emerged with identification of different ubiquitin chain topologies. However, mechanisms of how the diverse ubiquitin codes control biological processes remain poorly understood. Here, we use quantitative whole-proteome mass spectrometry to identify yeast proteins

Protocols

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

Chromatograms

application for HPLC

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