83833
Ribonuclease A from bovine pancreas
90%, powder, white, ~80 U/mg
Synonym(s):
Pancreatic Ribonuclease, RNAsea, RNase A, Ribonucleate 3′-pyrimidinooligonucleotidohydrolase
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-646-6
MDL number:
Specific activity:
~80 U/mg
Assay:
90%
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)
assay
90%
form
powder
specific activity
~80 U/mg
mol wt
~13,700, Mr ~13700
color
white
foreign activity
protease ≤0.001%
shipped in
wet ice
storage temp.
−20°C
Quality Level
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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)
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signalword
Danger
hcodes
pcodes
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
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Fabio Mohn et al.
Methods in molecular biology (Clifton, N.J.), 507, 55-64 (2008-11-07)
Methylated DNA immunoprecipitation (MeDIP) is a versatile immunocapturing approach for unbiased detection of methylated DNA. In brief, genomic DNA is randomly sheared by sonication and immunoprecipitated with a monoclonal antibody that specifically recognizes 5-methylcytidine. The resulting enrichment of methylated DNA
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
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
Pinaki P Misra et al.
Biopolymers, 97(12), 933-949 (2012-09-19)
In this study, we extensively report the effect of glycine betaine during the refolding of partially folded bovine α-lactalbumin (α-LA) in presence of hexadecyl trimethyl ammonium bromide (HTAB), and Ribonuclease A (RNAse A) in presence of sodium dodecyl sulfate (SDS)
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
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