Murine rnase inhibitor

Manufactured by Roche

Sourced in United States

The Murine RNase inhibitor is a laboratory reagent designed to prevent the degradation of ribonucleic acid (RNA) in biological samples. Its core function is to inhibit the activity of RNase enzymes, which can otherwise break down RNA molecules during experimental procedures.

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Lab products found in correlation

Protease phosphatase inhibitor cocktail, by Roche (1 mentions) 10 cm dishes, by Corning (1 mentions) Mini protease inhibitor tablet, by Roche (1 mentions) Np 40, by Thermo Fisher Scientific (1 mentions) Nebuffer 1, by Roche (1 mentions) Murine rnase inhibitor, by Vazyme (1 mentions) Nebuffer 2, by New England Biolabs (1 mentions) Lightcycler 96, by Roche (1 mentions)

Close spelling variants of this product

RNase inhibitor

3 protocols using murine rnase inhibitor

Orthogonal Cas12b and Cas13a Assays

Cited 2 times

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For the dsDNA target cleavage assay of AapCas12b, 1.2 μM AapCas12b protein, 1.2 μM sgRNA, 300 ng dsDNA substrate and 0.8 unit/μL Murine RNase Inhibitor (Vazyme, China) were incubated for 1 h at 60°C in cleavage buffer (NEBuffer 2.1, NEB, USA) as discribed.⁵⁴ (link)
For the ssRNA target cleavage assay of LwaCas13a, 0.6 μM LwaCas13a protein, 0.6 μM crRNA, 1300 ng ssRNA substrate and 0.8 unit/μL Murine RNase Inhibitor were incubated for 1 h at 37°C in NEBuffer 1.1 as discribed.⁹⁷ (link)
To test the orthogonal collateral cleavage of AapCas12b and LwaCas13a, 50 nM AapCas12b protein, 150 nM sgRNA, 10 nM dsDNA substrate, 0.8 unit/μL Murine RNase Inhibitor, 500 nM quenched ssDNA fluorescent probes and 500 nM quenched ssRNA fluorescent probes were incubated in NEBuffer 1.1 for 15 min at 60°C as discribed.⁵⁰ For LwaCas13a, an assay was performed with 50 nM LwaCas13a protein, 50 nM crRNA, 10 nM ssRNA substrate, 0.8 unit/μL Murine RNase Inhibitor, 500 nM quenched ssDNA fluorescent probes, 500 nM quenched ssRNA fluorescent probes and NEBuffer 1.1 for 15 min at 37°C as discribed.⁵⁰ The fluorescence signals of these reactions were recorded every minute by a LightCycler 96 (Roche, Swiss) in the FAM channel (for ssDNA probe) and ROX channel (for ssRNA probe). Detailed probe sequences are listed in Table S3.

Wang Z., Wang Y., Zhang Y., Qin G., Sun W., Wang A., Wang Y., Zhang G, & Zhao J. (2024). On-site detection and differentiation of African swine fever virus variants using an orthogonal CRISPR-Cas12b/Cas13a-based assay. iScience, 27(4), 109050.

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Cell Fractionation for Cytoplasm and Nucleus

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The cell fractionation assay was conducted according to a previous report [18 (link)]. Approximately 3 × 10⁶ cells were grown on 10 cm dishes (Corning), trypsinised, washed in cold 1x PBS, and centrifuged (1200 rpm, 5 min). Pellets were lysed in 1 mL hypotonic lysis buffer (10 mM HEPES pH 7.9, 10 mM KCl, 1.5 mM MgCl2, 1 mM β-mercaptoethanol, 0.075% NP-40, 1x murine RNase inhibitor, 1x protease/phosphatase inhibitor cocktails, Roche) and incubated for 15 min at 4°C with rotation. Nuclei were pelleted by centrifugation (1200 rpm, 4°C) for 15 min. The cytoplasm was collected from the supernatant. Nuclei were washed three times in 800 μL PBS and collected as the pelleted nuclear fraction. Fractionated cytoplasmic and nuclear lysates were confirmed by localization of GAPDH and histone 3.1, respectively.

Liu J., Li H., Wei C., Ding J., Lu J., Pan G, & Mao A. (2020). circFAT1(e2) Promotes Papillary Thyroid Cancer Proliferation, Migration, and Invasion via the miRNA-873/ZEB1 Axis. Computational and Mathematical Methods in Medicine, 2020, 1459368.

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Generation of G3BP1-mEmerald HeLa Cell Lysates

Cited 1 time

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The generation of cell lysates from G3BP1-mEmerald HeLa cells and the subsequent generation of lysate granules have been described previously^{15 (link)}. Briefly, cells were grown to 100% confluency in a 10 cm dish and harvested in 5 mL PBS. All steps were performed at room temperature. Collected cells were spun at 500 × g for 5 min with the supernatant aspirated and discarded. Cell pellets were stored at −80 °C until ready to use. To prepare cell lysates, pellets were thawed for 2 min and resuspended in 250 μL lysis buffer containing 50 mM TRIS pH7.0 (Sigma), 0.5% NP40 (Thermo), 0.025× mini protease inhibitor tablet (Roche) and 40× murine RNase inhibitor (NEB). After a 3-min incubation period lysates were spun at 24,000 × g for 5 min to remove nuclei and cell debris. The supernatant was retained to produce reconstituted stress granules when mixed with unlabelled G3BP1.

Erkamp N.A., Sneideris T., Ausserwöger H., Qian D., Qamar S., Nixon-Abell J., St George-Hyslop P., Schmit J.D., Weitz D.A, & Knowles T.P. (2023). Spatially non-uniform condensates emerge from dynamically arrested phase separation. Nature Communications, 14, 684.

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