83834
Ribonuclease A from bovine pancreas
4×cryst., ~70 U/mg (acc. to Kunitz)
Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
form
powder
Quality Level
quality
4×cryst.
specific activity
~70 U/mg (acc. to Kunitz)
mol wt
~13,700
Mr ~13700
impurities
proteases, none detected
shipped in
wet ice
storage temp.
−20°C
SMILES string
[nH]1cnc(c1)CC(NC(=O)CCN)C(=O)O
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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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.
Features and Benefits
Our highly stable Ribonuclease A, RNase A, is suitable for removal of RNA, RNA sequencing, and DNA purification.
Analysis Note
Protein determined by E.
Other Notes
1 U corresponds to the amount of enzyme which hydrolyzes the RNA at a rate constant k = 1 at 25°C and pH 5.0 (Kunitz-units); M. Kunitz, J. Biol. Chem. 164, 563 (1946)
Sales restrictions may apply
The enzyme only hydrolyzes phosphodiester linkages which originate from pyrimidine-3′-phosphates, as well as a large number of 2′,3′-cyclo compounds of cytidine and uridine derivatives; The return of pancreatic ribonucleases
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
Regulatory Information
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[On the mechanism of the ribonuclease reaction. 1. The function of the pyrimidine base in the reaction].
H G Gassen et al.
European journal of biochemistry, 1(1), 36-45 (1967-03-01)
S A Benner et al.
Trends in biochemical sciences, 14(10), 396-397 (1989-10-01)
A decade after losing favor as an 'uninteresting' digestive enzyme, pancreatic ribonuclease has been found to be homologous to a series of extracellular proteins that may influence tumor cell growth, neurological development and biological differentiation. One surprising outcome of these
Marka van Blitterswijk et al.
PloS one, 7(11), e48983-e48983 (2012-11-17)
Progressive muscular atrophy (PMA) and amyotrophic lateral sclerosis (ALS) are devastating motor neuron diseases (MNDs), which result in muscle weakness and/or spasticity. We compared mutation frequencies in genes known to be associated with MNDs between patients with apparently sporadic PMA
Chunju Li et al.
Journal of biotechnology, 162(2-3), 283-288 (2012-09-25)
Ribonuclease A (RNase A) is a therapeutic enzyme with cytotoxic action against tumor cells. Its clinical application is limited by the short half-life and insufficient stability. Conjugation of albumin can overcome the limitation, whereas dramatically decrease the enzymatic activity of
Yuen Lai Shek et al.
Biochemistry, 52(4), 672-680 (2013-01-09)
We report the first application of volume and compressibility measurements to characterization of interactions between cosolvents (osmolytes) and globular proteins. Specifically, we measure the partial molar volumes and adiabatic compressibilities of cytochrome c, ribonuclease A, lysozyme, and ovalbumin in aqueous
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