Athens Research/Cambio - Excellence in Molecular Biology/5 µg/µl 2 ml/MRNA092

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Enzymes for Molecular Biology

Enzymes for Molecular Biology: Enzymes for Molecular Biology

  • Catalogue
  • Description
  • Protocols
  • References
  • Notes
  • Applications & Benefits

RNase A

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues

BioSearch Tech (Lucigen/Epicentre)

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RNase A

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues

BioSearch Tech (Lucigen/Epicentre)

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues, forming oligoribonucleotides having 3"-terminal pyrimidine-3"-phosphates. Pyrimidine-3"-monophosphates are also released by RNase A cleavage of adjacent pyrimidine nucleotides.

Modified RNA containing pyrimidine-2"-fluoro-dNMPs, such as modified RNA made by in vitro transcription using the DuraScribe® T7 & SP6 Transcription Kits is completely resistant to cleavage by RNase A.

Composition and Concentration

Provided on the basis of weight at 5 mg/ml in Storage Buffer

Storage Buffer

50% glycerol containing 50 mM Tris-HCl (pH 7.5), 0.1 mM EDTA, 1 mM DDT, 0.1 M NaCl, and 0.1% Triton® X-100

Quality Control

RNase A is free of contaminating DNA exo- and endonuclease activities

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

RNase A

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues

BioSearch Tech (Lucigen/Epicentre)

protocol

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

RNase A

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues

BioSearch Tech (Lucigen/Epicentre)

References

  1. Johnson, M. (1996) EPICENTRE Forum 3(4), 7.
  2. Shen, V. and Schlessinger, D. (1982) The Enzymes XV (Part B), 501.
  3. delCardayré, S.B. and Raines, R.T. (1995) Anal. Biochem. 225, 176.

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

RNase A

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues

BioSearch Tech (Lucigen/Epicentre)

Epicentre® ForumGet your Epicentre® Forum - hot off the press!Click here for direct link to Forum listings

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

RNase A

Ribonuclease A (RNase A) is an endoribonuclease that cleaves single-stranded RNA at the 3"-end of pyrimidine residues

BioSearch Tech (Lucigen/Epicentre)

Applications

  • Removal of RNA from DNA preparations.1
  • RNase protection assays to detect single-basepair mismatches in RNA:RNA and RNA:DNA hybrids.1

If you cannot find the answer to your problem below then please contact us or telephone 01954 210 200

Myeloperoxidase Enzyme Immunoassay Kit 髓过氧化物酶 免疫分析试剂盒 Human MPO EIA KIT FEATURES: USE - Measure human MPO in a variety of matrices SAMPLE -Serum, Platelet-Poor Heparin Plasma, Saliva, Urine or Tissue Culture Media SAMPLES / KIT - 40 in duplicate SENSITIVITY - 0.068 ng/mL STABILITY - liquid reagents stable at 4°C QUICK RESULTS - 2.5 HOURS Myeloperoxidase (MPO) is a tetrameric heme-containing protein abundantly produced in neutrophil granulocytes where it plays an important anti-microbial role. During degranulation MPO is released into the extracellular space. There, as part of the neutrophils “respiratory burst”, it produces hypochlorous acid from hydrogen peroxide and Cl–. MPO also uses hydrogen peroxide to oxidize tyrosine to the tyrosyl radical. Both hypochlorous acid and tyrosyl are cytotoxic and when present can kill bacteria and other pathogens. Hereditary deficiency of myeloperoxidase predisposes individuals to immune deficiency. Studies have shown an association between elevated MPO levels and coronary artery disease, and in 2003 it was suggested that MPO may serve as a sensitive predictor of myocardial infarction in patients complaining of chest pain. Since that time the clinical utility of MPO testing in cardiac patients has been solidly established in the literature with well over 100 papers published. In 2010 this clinical application was further refined by additional studies which determined that measuring both MPO and C-reactive protein (CRP) provided more accurate prediction of mortality risk than measuring just CRP alone.