Pierce™ Universal Nuclease for Cell Lysis
Pierce™ Universal Nuclease for Cell Lysis
Actual product may vary
Thermo Scientific™

Pierce™ Universal Nuclease for Cell Lysis

Thermo Scientific Pierce Universal Nuclease for Cell Lysis is ideal for a wide variety of applications where complete digestion ofRead more
Catalog NumberQuantity
88702100 kU
887005 kU
8870125 kU
Catalog number 88702
Price (JPY)
115,000
Each
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Quantity:
100 kU
Request bulk or custom format
Thermo Scientific Pierce Universal Nuclease for Cell Lysis is ideal for a wide variety of applications where complete digestion of nucleic acids is needed when preparing cell lysates.

Features of Universal Nuclease for Cell Lysis:

Broad spectrum—degrades all forms of DNA and RNA
Highest-quality enzyme—nuclease is ≥99% pure, as tested by SDS-PAGE
Robust activity—100-fold greater specific activity than DNase I
Versatile—can be used with a wide variety of cell lysis reagents

Pierce Universal Nuclease for Cell Lysis is a genetically engineered endonuclease from Serratia marcescens. The enzyme is produced and purified from E. coli and consists of two identical 30-kDa subunits with two critical disulfide bonds. This indiscriminate endonuclease degrades single-stranded, double-stranded, linear and circular DNA and RNA and is effective over a wide range of temperatures and pH. This enzyme has high specific activity (100-fold greater than DNase I) and increased thermal stability compared to other nucleases. Pierce Universal Nuclease is ≥99 pure enzyme, is free of any measurable protease activity and is supplied at 250U/μL. Pierce Universal Nuclease for Cell Lysis is identical in performance to Benzonase™ Nuclease (EMD Merck).

Applications:
• Use with B-PER, Y-PER or other commercial or homebrew cell lysis reagents and/or mechanical disruption to reduce viscosity in protein extracts
• Remove DNA and RNA from recombinant protein preparations prior to downstream processing

Pierce Universal Nuclease for Cell Lysis is commonly used to reduce the viscosity of bacterial and mammalian protein extracts for downstream application by removing the nucleic acids from protein preparations. The enzyme completely digests nucleic acids to oligonucleotides that are less than 5 bases long. Pierce Universal Nuclease for Cell Lysis helps to improve the separation of the lysate pellet from the supernatant, enhances filtration of the treated lysate, improves chromatography processing time and increases the overall protein yield. The endonuclease has also been shown to improve the compatibility of protein extracts for 2D gel electrophoresis. One unit corresponds to the amount of enzyme required to produce a change of 1.0 in the absorbance at 260nm of sonicated Herring DNA over 30 minutes at 37°C, as determined using standard nuclease from the Merck™ Serratia marcescens volumetric activity assay.

Related Products
Micrococcal Nuclease Solution (≥ 1 unit/μL)
For Research Use Only. Not for use in diagnostic procedures.
Specifications
EnzymeNuclease
Quantity100 kU
Reagent TypeEnzyme for Cell Lysis
FormLiquid
Product LinePierce
Product TypeCell Lysis Enzyme
Unit SizeEach
Contents & Storage
Store in a cool, dry, well-ventilated area, protected from direct sunlight.

Frequently asked questions (FAQs)

After cell lysis, my mass spectrometry sample is very viscous and difficult to pipette. How do I reduce the sample viscosity?

High sample viscosity after lysis is due to release of DNA from the nucleus. Sonication or addition of a nuclease such as the Pierce Universal Nuclease (Cat. No. 88700, 88701, or 88702) can be used to degrade DNA and reduce sample viscosity.

Find additional tips, troubleshooting help, and resources within our Mass Spectrometry Support Center.

Can you explain how the B-PER Bacterial Protein Extraction Reagent lyses cells?

The B-PER Reagent solution contains a proprietary, mild, non-ionic detergent in 20 mM Tris-HCl, pH 7.5. It effectively disrupts cells and solubilizes native or recombinant proteins without denaturation. The reagent creates holes in the cell membrane that will leak out cytosolic proteins. The sample may become very viscous when the bacterial chromosome is released. We recommend adding DNAse I (Cat. No. 90083) to the reagent to reduce viscosity. For better lysis efficiency and if there are inclusion bodies, we recommend adding Lysozyme (Cat. No. 90082) to the reagent. Alternatively, you may purchase the B-PER Bacterial Protein Extraction Reagent with Enzymes Kit (Cat. No. 90078 or 90079) that includes the B-PER Bacterial Protein Extraction Reagent, DNase I, and Lysozyme.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Citations & References (4)

Citations & References
Abstract
Site-specific incorporation of citrulline into proteins in mammalian cells.
Authors:Mondal S,Wang S,Zheng Y,Sen S,Chatterjee A,Thompson PR
Journal:Nature communications
PubMed ID:33398026
Citrullination is a post-translational modification (PTM) of arginine that is crucial for several physiological processes, including gene regulation and neutrophil extracellular trap formation. Despite recent advances, studies of protein citrullination remain challenging due to the difficulty of accessing proteins homogeneously citrullinated at a specific site. Herein, we report a technology ... More
Genetically encoded protein sulfation in mammalian cells.
Authors:Italia JS,Peeler JC,Hillenbrand CM,Latour C,Weerapana E,Chatterjee A
Journal:Nature chemical biology
PubMed ID:32198493
Tyrosine sulfation is an important post-translational modification found in higher eukaryotes. Here we report an engineered tyrosyl-tRNA synthetase/tRNA pair that co-translationally incorporates O-sulfotyrosine in response to UAG codons in Escherichia coli and mammalian cells. This platform enables recombinant expression of eukaryotic proteins homogeneously sulfated at chosen sites, which was demonstrated ... More
Discrimination and surveillance of infectious severe acute respiratory syndrome Coronavirus 2 in wastewater using cell culture and RT-qPCR.
Authors:Monteiro S,Rente D,Cunha MV,Marques TA,Cardoso E,Vilaça J,Coelho N,Brôco N,Carvalho M,Santos R
Journal:The Science of the total environment
PubMed ID:34999067
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) RNA has been extensively detected in raw wastewater in studies exploring wastewater-based epidemiology (WBE) for early warning purposes. Nonetheless, only a few limited studies investigated the presence of SARS-CoV-2 in treated wastewaters to determine the potential health risks across the water cycle. The ... More
p53 is active in murine stem cells and alters the transcriptome in a manner that is reminiscent of mutant p53.
Authors:Yan H, Solozobova V, Zhang P, Armant O, Kuehl B, Brenner-Weiss G, Blattner C
Journal:
PubMed ID:25719246
Since it was found that p53 is highly expressed in murine embryonic stem cells, it remained a mystery whether p53 is active in this cell type. We show that a significant part of p53 is localised in the nucleus of murine embryonic stem cells and that the majority of this ... More