Pierce™ Universal Nuclease for Cell Lysis
Pierce™ Universal Nuclease for Cell Lysis
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
Have Questions?
Change viewbuttonViewtableView
Catalog NumberQuantity
887005 kU
88702100 kU
8870125 kU
Catalog number 88700
Price (USD)
74.65
Online Exclusive
82.00
Save 7.35 (9%)
5 kU
In stock
Add to cart
Quantity:
5 kU
Recurring order eligible. Learn more »
Request bulk or custom format
Price (USD)
74.65
Online Exclusive
82.00
Save 7.35 (9%)
5 kU
Add to cart
Ask our AI about this Product
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
DescriptionPierce Universal Nuclease for Cell Lysis
EnzymeNuclease
FormulationAt least 99% pure enzyme at 250 U/uL in 50% glycerol (v/v), 20 mM NaCl, 2 mM MgCl2, 20 mM Tris, pH 8.0
Quantity5 kU
Reagent TypeEnzyme for Cell Lysis
Sufficient For200 mL Lysate
FormLiquid
Product LinePierce™
Product TypeCell Lysis Enzyme
Unit Size5 kU
Contents & Storage
Store in a cool, dry, well-ventilated area, protected from direct sunlight.
Have questions about this product? Ask our AI assisted search.
This is an AI-powered search and may not always get things right. You can help us make it better with a thumbs up or down on individual answers or by selecting the “Give feedback" button. Your search history and customer login information may be retained by Thermo Fisher and processed in accordance with our Privacy Notice.

Figures

Customers who viewed this item also viewed



Documents & Downloads

Certificates

Lot #Certificate TypeDateCatalog Number(s)
3269151Certificate of AnalysisJun 26, 202588701
3257568Certificate of AnalysisJun 10, 202588700
3250263Certificate of AnalysisMay 30, 202588702
3247573Certificate of AnalysisMay 27, 202588701
3246890Certificate of AnalysisMay 26, 202588701
5 results displayed, search above for a specific certificate

Safety Data Sheets

Frequently asked questions (FAQs)

We would suggest the following procedure (note that you should determine yourself empirically the optimal incubation time, incubation temperature and also dilution): Please add 25 U or 0.1 µL Pierce Universal Nuclease for Cell Lysis (Cat. No. 88700) to 1 mL of cell lysate (dilution 1:10,000) and incubate at room temperature for 10-15 minutes. If you want to dilute the Nuclease for facilitating pipetting, please do this with Tris- or PBS-buffer at pH 7-8.

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

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.

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 (8)

Citations & References
Abstract
Validation of an IFN-gamma ELISpot assay to measure cellular immune responses against viral antigens in non-human primates.
Authors:Yang F,Patton K,Kasprzyk T,Long B,Gupta S,Zoog SJ,Tracy K,Vettermann C
Journal:Gene therapy
PubMed ID:33432123
Adeno-Associated Virus (AAV)-based gene therapy vectors are in development for many inherited human disorders. In nonclinical studies, cellular immune responses mediated by cytotoxic T cells may target vector-transduced cells, which could impact safety and efficacy. Here, we describe the bioanalytical validation of an interferon-gamma (IFN-γ)-based Enzyme-Linked Immunospot (ELISpot) assay for ... More
Characterization of an expanded set of assays for immunomodulatory proteins using targeted mass spectrometry.
Authors:Whiteaker JR,Zhao L,Schoenherr RM,Huang D,Kennedy JJ,Ivey RG,Lin C,Lorentzen TD,Colantonio S,Caceres TW,Roberts RR,Knotts JG,Reading JJ,Perry CD,Garcia-Buntley SS,Bocik W,Hewitt SM,Paulovich AG
Journal:Scientific data
PubMed ID:38918394
Immunotherapies are revolutionizing cancer care, but many patients do not achieve durable responses and immune-related adverse events are difficult to predict. Quantifying the hundreds of proteins involved in cancer immunity has the potential to provide biomarkers to monitor and predict tumor response. We previously developed robust, multiplexed quantitative assays for ... More
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
PhoXplex: Combining Phospho-enrichable Cross-Linking with Isobaric Labeling for Quantitative Proteome-Wide Mapping of Protein Interfaces.
Authors:Hoenger Ramazanova RD,Roumeliotis TI,Wright JC,Choudhary JS
Journal:Journal of proteome research
PubMed ID:39422127
Integrating cross-linking mass spectrometry (XL-MS) into structural biology workflows provides valuable information about the spatial arrangement of amino acid stretches, which can guide elucidation of protein assembly architecture. Additionally, the combination of XL-MS with peptide quantitation techniques is a powerful approach to delineate protein interface dynamics across diverse conditions. While ... More
8 total citations

Other products to consider



Share catalog number, name or link

1x1 image pixel for data collection