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Merck
CN

R5125

Ribonuclease A from bovine pancreas

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

Synonym(s):

Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase

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About This Item

CAS Number:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
232-646-6
MDL number:
EC Number:
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Product Name

Ribonuclease A from bovine pancreas, Type III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein

SMILES string

[nH]1cnc(c1)CC(NC(=O)CCN)C(=O)O

InChI key

CQOVPNPJLQNMDC-UHFFFAOYSA-N

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)

biological source

bovine pancreas

type

Type III-A

assay

≥85% RNase A basis (SDS-PAGE)

form

lyophilized powder

specific activity

85-140 Kunitz units/mg protein

mol wt

~13,700

technique(s)

cell based assay: suitable

impurities

salt, essentially free

suitability

suitable for molecular biology

application(s)

diagnostic assay manufacturing

foreign activity

protease, essentially free

storage temp.

−20°C

Quality Level

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Analysis Note

Protein determined by E.

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 nickel-dependent oxidative cross-linking of a protein. Ribonuclease A from bovine pancreas has also been used in a study to investigate equilibrium constants for nonspecific binding of proteins to DNA.

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.

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.

Preparation Note

Salt fractionated and chromatographically purified.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

低风险生物材料
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G Gill et al.
Chemical research in toxicology, 10(3), 302-309 (1997-03-01)
A model protein, ribonuclease A (bovine pancreas), was examined for its ability to coordinate Ni2+ and promote selective oxidation. In the presence of a peracid such as monopersulfate, HSO5-, nickel induced the monomeric RNase A to form dimers, trimers, tetramers
E S Jenuwine et al.
Analytical biochemistry, 242(2), 228-233 (1996-11-15)
Quantitative zonal DNA affinity chromatography may be used to determine accurate equilibrium constants for the binding of proteins nonspecifically to DNA. Zonal quantitative affinity chromatography has not previously been applied to the determination of binding constants of proteins to DNA
J Yu et al.
Cytometry, 14(4), 428-432 (1993-01-01)
DNA content by flow cytometry was assessed in 47 cases from a series of 130 patients with non-small cell lung carcinoma (NSCLC) given radiation therapy postoperatively. This was done in an attempt to identify which patients might benefit, or not
J Castro et al.
Cytometry, 14(7), 793-804 (1993-10-01)
An easy method for preparation of bare cell nuclei from fresh solid tissues for DNA flow cytometry is described. Pieces of up to 2 x 2 x 2 mm3 size from fresh tissues were fixed in formalin. After removal of
Thomas Blasi et al.
Nature communications, 7, 10256-10256 (2016-01-08)
Imaging flow cytometry combines the high-throughput capabilities of conventional flow cytometry with single-cell imaging. Here we demonstrate label-free prediction of DNA content and quantification of the mitotic cell cycle phases by applying supervised machine learning to morphological features extracted from

Protocols

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

本实验方案可用于测定核糖核酸酶A(RNase A)的活性。

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