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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

type

Type I-AS

Quality Level

form

lyophilized powder

specific activity

50-100 Kunitz units/mg protein

mol wt

~13,700

impurities

salt, essentially free

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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1 of 4

This Item
R5125R5500R5000
specific activity

50-100 Kunitz units/mg protein

specific activity

85-140 Kunitz units/mg protein

specific activity

75-125 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

application(s)

diagnostic assay manufacturing

application(s)

diagnostic assay manufacturing

application(s)

-

application(s)

diagnostic assay manufacturing

foreign activity

protease, essentially free

foreign activity

protease, essentially free

foreign activity

protease, essentially free

foreign activity

-

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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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
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
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
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
Bryan E McQueen et al.
Infection and immunity, 88(9) (2020-07-01)
Chlamydia trachomatis infection of the human fallopian tubes can lead to damaging inflammation and scarring, ultimately resulting in infertility. To study the human cellular responses to chlamydial infection, researchers have frequently used transformed cell lines that can have limited translational

Protocols

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

Chromatograms

application for HPLC

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