OmniCleave™ Endonuclease is a highly purified enzyme from a recombinant E. coli strain that degrades single- and double-stranded DNA and RNA to di-, tri-, and tetranucleotides(Figure 1). OmniCleave™ Endonuclease has the same substrate specificity and yields the same products as benzonase®, an enzyme derived from Serratia marcescens.

Figure 1. Removal of nucleic acids from cell lysates using OmniCleave™ Endonuclease. Cell lysates were prepared with or without OmniCleave Endonuclease from E. coli cells expressing human lactate dehydrogenase B (LDH) and E. coli alkaline phosphatase (AP). Two microliters of each of the cell lysates were separated by electrophoresis on a 1% agarose gel and the nucleic acids detected by ethidium bromide staining. Lane M, 1-kb ladder

Unit Definition:

One unit converts 1.0 OD260 (~60µg) of salmon sperm DNA into acid-soluble nucleotides in 30 minutes at 37°C in 50mM Tris-HCl, pH 8.0 at 25°C and 1mM MgCl₂.

Storage Buffer:

50% glycerol solution containing 50mM Tris-HCl, pH 7.5 at 25°C, 0.1M NaCl, 0.1mM EDTA, 1mM dithiothreitol, and 0.1% Triton® X-100.

Quality Control:

OmniCleave™ Endonuclease is free of detectable protease activity.

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Protocols for: OmniCleave™ Endonuclease

Due to the constant updating of the protocols by the manufacturer we have provided a direct link to Epicentre’s product page, where the latest protocol is available.

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OmniCleave™ Endonuclease Protocol

(catalogue number OC7810K / OC7850K)

Please note: all protocols off site are the responsibility of the products supplier

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References

1. Molloy, MP. et al. (1998) Electrophoresis 19, 837.
2. Herbert, BR. et al. (1998) Electrophoresis 19, 851.
3. Chandramouli, S., et al. (2010) Serotype-Specific Structural Differences in the Protease-Cofactor Complexes of the Dengue Virus Family, J. Virol. 84 , 3059-3067.
4. van Leeuwen, M., et al. (2010) Human Picobirnaviruses Identified by Molecular Screening of Diarrhea Samples, J. Clin. Microbiol. 48 , 1787-1794.
5. Gilljam, K. M., et al. (2009) Identification of a novel, widespread, and functionally important PCNA-binding motif, J. Cell Biol. 186 , 645-654.
6. Pelish, T. M. & McClain, M. S. (2009) Dominant-negative Inhibitors of the Clostridium perfringens {epsilon}-Toxin, J. Biol. Chem. 284 , 29446-29453.
7. Otterlei, M., et al. (2006) Werner syndrome protein participates in a complex with RAD51, RAD54, RAD54B and ATR in response to ICL-induced replication arrest, J. Cell Sci. 119 , 5137-5146.
8. Torres, V. J., et al. (2005) Functional Properties of the p33 and p55 Domains of the Helicobacter pylori Vacuolating Cytotoxin, J. Biol. Chem. 280 , 21107-21114.
9. Fan, J., et al. (2004) XRCC1 co-localizes and physically interacts with PCNA, Nucleic Acids Res. 32 , 2193-2201.
10. Guarino, L. A., et al. (2002) Baculovirus lef-12 Is Not Required for Viral Replication, J. Virol. 76 , 12032-12043.
11. Sawitzke, J. A., et al. (2002) Transcriptional Interference by a Complex Formed at the Centromere-Like Partition Site of Plasmid P1, J. Bacteriol. 184 , 2447-2454.
12. Feilmeier, B. J., et al. (2000) Green Fluorescent Protein Functions as a Reporter for Protein Localization in Escherichia coli, J. Bacteriol. 182 , 4068-4076.
13. Feltzer, R. E., et al. (2000) Alkaline Proteinase Inhibitor of Pseudomonas aeruginosa.Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases, J. Biol. Chem. 275 , 21002-21009.

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

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