83834
Ribonuclease A from bovine pancreas
4×cryst., ~70 U/mg (acc. to Kunitz)
Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
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About This Item
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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
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.
Unit Definition
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)
Analysis Note
Protein determined by E.
Other Notes
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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
Shuangsheng Huang et al.
International journal of molecular medicine, 30(6), 1410-1416 (2012-10-03)
Tumor cells trigger angiogenesis through overexpression of various angiogenic factors including vascular endothelial growth factor (VEGF) and angiopoietin 1 (Ang1). Therefore, inhibition of the expression of both VEGF and Ang1, the initial step of tumor angiogenesis, is a promising strategy
Caterina Brandmayr et al.
Angewandte Chemie (International ed. in English), 51(44), 11162-11165 (2012-10-06)
Useful diversity: Quantification of modified tRNA nucleobases in different murine and porcine tissues reveals a tissue-specific overall modification content. The modification content correlates with rates of protein synthesis in vitro, suggesting a direct link between tRNA modification levels and tissue-specific translational
Influence of thyroid state on cardiac and renal capillary density and glomerular morphology in rats.
Isabel Rodríguez-Gómez et al.
The Journal of endocrinology, 216(1), 43-51 (2012-10-11)
The purpose was to analyse the cardiac and renal capillary density and glomerular morphology resulting from a chronic excess or deficiency of thyroid hormones (THs) in rats. We performed histopathological, morphometrical and immunohistochemical analyses in hypothyroid and hyperthyroid rats to
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