Pierce™ Universal Nuclease for Cell Lysis
Pierce™ Universal Nuclease for Cell Lysis
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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 ofLeia mais
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Número do catálogoQuantity
8870125 kU
887005 kU
88702100 kU
Número do catálogo 88701
Preço (BRL)
1.848,64
Each
Adicionar ao carrinho
Quantity:
25 kU
Request bulk or custom format
Preço (BRL)
1.848,64
Each
Adicionar ao carrinho
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.
Especificações
BufferLysis Buffer
EnzymeNuclease
Quantity25 kU
Reagent TypeEnzyme for Cell Lysis
FormLiquid
Product LinePierce
Product TypeCell Lysis Enzyme
Unit SizeEach
Conteúdo e armazenamento
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.

Citações e referências (5)

Citações e referências
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
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
An efficient and cost-effective purification protocol for Staphylococcus aureus Cas9 nuclease.
Authors:Teng ACT,Tavassoli M,Shrestha S,Marks RM,McFadden MJ,Evagelou SL,Lindsay K,Vandenbelt A,Li W,Ivakine E,Cohn R,Santerre JP,Gramolini AO
Journal:STAR protocols
PubMed ID:36574341
Here, we describe a protocol for purifying functional clustered regularly interspaced short palindromic repeats (CRISPR)-associated protein 9 (Cas9) from Staphylococcus aureus within 24 h and over 90% purity. SaCas9 purification begins with immobilized metal affinity chromatography, followed by cation exchange chromatography, and ended with centrifugal concentrators. The simplicity, cost-effectiveness, and reproducibility ... 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