Ribonuclease A (RNase A) - DNase-free

RNase A - Ribonuclease


Order number: S5218.0050

Shipping: shipped at RT, stored at -20°C
CAS-Nr: 9001-99-4

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Ribonuclease A- DNase-free is a DNase and Protease-free enzyme that can be used directly for RNA... more
Product information "Ribonuclease A (RNase A) - DNase-free"

Ribonuclease A- DNase-free is a DNase and Protease-free enzyme that can be used directly for RNA digests. Elimination of potential DNAse activity is not necessary. Potential DNAse activities have been removed.

Ribonuclease A is an endo-ribonuclease specifically cleaving single stranded RNA at the 3' side of pyrimidine bases (cytosine and uracil). RNAse A ist used to prepare RNA-free DNA, to digest non-hybridised regions of RNA-DNA hybrids and as a molecular weight marker. The pH optimum for RNAse A is between 7.0-7.5. RNAse A is inhibited by Diethylpyrocarbonate (DEPC) >, guanidinium salt (4M GuaSCN), beta-Mercaptoethanol, heavy metals, vanadyl-ribonucleoside complexes, RNAse-inhibitor from human placenta and by competitive DNA. RNAse A cleaves single and douple stranded RNA and RNA in RNA:DNA hybrids at low salt conditions (100mM NaCl). At high salt conditions (>300 mM NaCl), RNAse A cleaves single-stranded RNA only. The enzyme can only be removed by Proteinase K digest and subsequent phenol extraction.

Stock solution: Stock solutions are prepared at concentrations from 1 - 10mg/mL in 10mM Tris/HCl, pH7.5; 15mM NaCl or in 10mM Tris/HCl, pH7.5; 1mM EDTA, pH8.0 (TE buffer).
The recommended working concentration is 10µg/mL (removal of RNA from plasmid preparations; 1hr, RT) or 100ng/mL (preparation of 'blunt ends' of double-stranded cDNA).

Stability:RNase A aggregates during lyophilizing and storage. It has a high affinity to glas surfaces, which has to be taken into consideration. At neutral pH (e. g. in PBS pH 7.4) and high concentrations (>10mg/mL) the enzyme will precipitate. At +2°C to +8°C (lyophilized) it is stable for several years (dry storage), in solution (-20°C) several years or (+2°C to +8°C) several weeks.

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Our comment on "Ribonuclease A (RNase A) - DNase-free"
DNase-free Protease-free
Specifications: Activity: min. 80 kunits/mg DNases: not detectable Proteases: not detectable... more
 

Technical Data:

Specifications:
Activity: min. 80 kunits/mg
DNases: not detectable
Proteases: not detectable
MW = approx. 13,700 Da
Product is isolated from BSE free source.

Optimal temperature: 60°C (activity range of 15–70°C); Optimal pH: 7.6 (activity range of 6–10); Inhibitors: ribonuclease inhibitor. Activators of RNase A: potassium and sodium salts.

application:

RNase protection assays Remove unspecifically bound RNA Analysis of RNA sequences Hydrolyze RNA contained in protein samples Purification of DNA Pancreatic RNase A specifically cleaves at the 3'-side of pyrimidine (uracil or cytosine) phosphate bonds

Unit Definition:

1 unit corresponds to the amount of enzyme which hydrolyzes RNA at a rate constant k = 1 at 25°C and pH 5.0 (Kunitz-units), M. Kunitz, J. Biol. Chem. 164, 563 (1946).

Source

bovine pancreas

Sicherheits Hinweise / Safety

Klassifizierungen / Classification

EC-Nr: 232-646-6
CAS-Nr: 9001-99-4
eclass-Nr: 32-16-04-10
Dokumente - Protokolle - Downloads more

Dokumente - Protokolle - Downloads

Here you will find information and further literature on Ribonuclease A (RNase A) - DNase-free. For further documents (certificates with additional lot numbers, safety data sheets in other languages, further product information) please contact Genaxxon biosience at: info@genaxxon.com or phone: +49 731 3608 123.

 
 
 
Literatur .... more

Referenzen..

Hier finden Sie Artikel und Literaturzitate, in denen die Autoren auf die hohe Qualität dieses Genaxxonprodukts vertrauen.
Listed below are articles and references, in which the authors trust in the high quality of this Genaxxon product.

Quelle/Source: NCBI PubMed >

Native matrix-based human lung alveolar tissue model in vitro: studies of the reparatory actions of mesenchymal stem cells

Ieva Bruzauskaite, Jovile Raudoniute, Jaroslav Denkovskij, Edvardas Bagdonas, Sandra Meidute-Abaraviciene, Vaida Simonyte, Daiva Bironaite, Almantas Siaurys, Eiva Bernotiene, Ruta Aldonyte

Cytotechnology. 2017 Feb; 69(1): 1–17. Published online 2016 Dec 1. doi: 10.1007/s10616-016-0021-z

PMCID: PMC5264619