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Chloroquine solution

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Chloroquine solution is a laboratory reagent produced by Merck Group. It is an aqueous solution containing the chemical compound chloroquine, which is commonly used in scientific research and analysis. The core function of this product is to serve as a standardized solution for various applications, such as chemical testing and analysis. No further details or interpretations are provided.

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Lab products found in correlation

Blasticidin, by Thermo Fisher Scientific (4 mentions) Facscalibur, by BD (3 mentions) Polybrene, by Merck Group (3 mentions) Puromycin, by Serva Electrophoresis (3 mentions) Mg132 solution, by Merck Group (1 mentions) Polybrene solution, by Merck Group (1 mentions)

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Chloroquine (1238 citations)

5 protocols using chloroquine solution

1

Efficient Retroviral Transduction of Phoenix Cells

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5 × 106Phoenix™ cells were seeded and 24 h later they were transfected with the plasmid DNA of choice. Briefly, 20 μg of DNA were mixed with 860 μL of H2O and 120 μL of 2 M CaCl2 and mixed by vortexing. The DNA solution was transferred dropwise to 1 mL of 2 × HBS buffer (50 mM HEPES pH 7.05, 10 mM KCl, 12 mM Glucose, 280 mM NaCl, 1.5 mM NaHPO4) while vortexing and the solution was incubated 20 min at room temperature. In the meantime, 25 μM Chloroquine solution (Sigma-Aldrich) was added to the Phoenix™ cells (1 μl/ml) and the cells were incubated for 10 min. The DNA solution was added to the cells and 12 h later the medium was replaced. After 24 h of incubation, the medium containing the retroviral suspension was filtered and Polybrene (Sigma-Aldrich) solution was added. Fresh medium was added to the Phoenix™ cells that were maintained in culture for further infections. The retroviral solution was used for spin infection of MT cells by centrifuging 45 min at 1800 rpm at 37°C. In total, four spin infections were performed over two days. Positively infected cells were selected with puromycin (Serva) or blasticidin (GIBCO) and, eventually, GFP positivity was analyzed using a BD FACS Calibur
Yuan Z., VanderWielen B.D., Giaimo B.D., Pan L., Collins C.E., Turkiewicz A., Hein K., Oswald F., Borggrefe T, & Kovall R.A. (2019). Structural and Functional Studies of the RBPJ-SHARP Complex Reveal a Conserved Corepressor Binding Site. Cell reports, 26(4), 845-854.e6.
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2

CRISPR/Cas9-Mediated RBPJ Depletion in Murine Hybridoma T-Cells

Cited 1 time
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CRISPR/Cas9-mediated RBPJ depleted mouse hybridoma mature T-cells were generated as previously described (Yuan et al., 2019 (link)). T-cell lines stably expressing RBPJwt, phospho-deficient (S-to-A) or phospho-mimetic (S-to-D) RBPJ-mutant depleted MT-cells were generated as follows: 5 × 106 PhoenixTM cells were seeded and 24 h later they were transfected with the retroviral plasmid DNA without insert (control) or containing RBPJwt, RBPJS221A or RBPJS221D. Briefly, 20 μg of DNA were mixed with 860 μl of H2O and 120 μl of 2x HBS buffer (50 mM HEPES pH 7.05, 10 mM KCl, 12 mM Glucose, 280 mM NaCl, 1.5 mM NaHPO4) while vortexing and the solution was incubated 20 min at room temperature. In the meantime, 25 μM Chloroquine solution (Sigma-Aldrich) was added to the PhoenixTM cells (1 μl/ml) and the cells were incubated for 10 min. The DNA solution was added to the cells and 12 h later the medium was replaced. After 24 h of incubation, the medium containing the retroviral suspension was filtered and Polybrene (Sigma-Aldrich) solution was added. Fresh medium was added to the PhoenixTM cells that were maintained in culture for further infections. The retroviral solution was used for spin infection of MT cells by centrifuging 45 min at 1800 rpm at 37°C. In total, four spin infections were performed over 2 days. Positively infected cells were selected with Blasticidin (Gibco).
Frankenreiter L., Gahr B.M., Schmid H., Zimmermann M., Deichsel S., Hoffmeister P., Turkiewicz A., Borggrefe T., Oswald F, & Nagel A.C. (2021). Phospho-Site Mutations in Transcription Factor Suppressor of Hairless Impact Notch Signaling Activity During Hematopoiesis in Drosophila. Frontiers in Cell and Developmental Biology, 9, 658820.
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3

Proteasome Inhibition Effects on Cell Cycle

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A 10 µM chloroquine solution (2x) (Sigma Chemical Co., St. Louis, MO, USA), a 10 mM MG132 solution (2x) (Sigma Chemical Co., St. Louis, MO, USA), and a 25 µM EMD638683 solution (2x) (Cayman Chemical Co., Ann Arbor, MI, USA) were prepared in PBS (137 mM NaCl, 2.7 mM KCl, 8 mM Na2HPO4, and 2 mM KH2PO4) from concentrated solutions diluted in dimethyl sulfoxide (DMSO) to achieve a final DMSO concentration of 0.02%. Indeed, the additional effects of proteasome inhibitors on cell cycle progression and induction of apoptosis are well-known. However, the concentration and duration of incubation we used had the desired effect of inhibiting the chymotrypsin-like activity of the proteasome [41 (link)].
Ríos-Medina Y., Rico-Chávez P., Martínez-Vieyra I., Durán-Álvarez J.C., Rodriguez-Varela M., Rincón-Heredia R., Reyes-López C, & Cerecedo D. (2024). Altered Plasma Membrane Lipid Composition in Hypertensive Neutrophils Impacts Epithelial Sodium Channel (ENaC) Endocytosis. International Journal of Molecular Sciences, 25(9), 4939.
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4

Phoenix Cell Transfection and Retroviral Infection

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5 × 106 Phoenix™ cells were seeded and 24 h later cells were transfected with the plasmid DNA of choice. Briefly, 20 μg of DNA were mixed with 860 μl of H2O and 120 μl of 2 M CaCl2 by vortexing. The DNA solution was transferred dropwise to 1 ml of 2× HBS buffer (50 mM HEPES pH 7.05, 10 mM KCl, 12 mM glucose, 280 mM NaCl, 1.5 mM NaHPO4) while vortexing and the solution was incubated 20 min at room temperature. In the meantime, 1 μl/ml of 25 μM Chloroquine solution (Sigma-Aldrich) were added to the Phoenix™ cells and the cells were incubated for 10 min at room temperature. The DNA solution was added to the cells and after 12 h of incubation at 37°C with 5% CO2, the medium was replaced with fresh one. After 24 h of incubation, the medium containing the retroviral suspension was filtered and 1 μl/ml of 2 mg/ml Polybrene solution (Sigma-Aldrich) were added. Fresh medium was added to the Phoenix™ cells that were kept in culture for further infections. The retroviral solution was used for spin infection of MT cells by centrifuging 45 min at 1800 rpm at 37°C. In total, four spin infections were performed over 2 days. Positively infected cells were selected with puromycin (Serva) or blasticidin (Gibco) and, eventually, GFP positivity was analyzed using a BD FACS Calibur.
Friedrich T., Ferrante F., Pioger L., Nist A., Stiewe T., Andrau J.C., Bartkuhn M., Giaimo B.D, & Borggrefe T. (2022). Notch-dependent and -independent functions of transcription factor RBPJ. Nucleic Acids Research, 50(14), 7925-7937.
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5

Efficient Retroviral Transduction of Phoenix Cells

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5 × 106Phoenix™ cells were seeded and 24 h later they were transfected with the plasmid DNA of choice. Briefly, 20 μg of DNA were mixed with 860 μL of H2O and 120 μL of 2 M CaCl2 and mixed by vortexing. The DNA solution was transferred dropwise to 1 mL of 2 × HBS buffer (50 mM HEPES pH 7.05, 10 mM KCl, 12 mM Glucose, 280 mM NaCl, 1.5 mM NaHPO4) while vortexing and the solution was incubated 20 min at room temperature. In the meantime, 25 μM Chloroquine solution (Sigma-Aldrich) was added to the Phoenix™ cells (1 μl/ml) and the cells were incubated for 10 min. The DNA solution was added to the cells and 12 h later the medium was replaced. After 24 h of incubation, the medium containing the retroviral suspension was filtered and Polybrene (Sigma-Aldrich) solution was added. Fresh medium was added to the Phoenix™ cells that were maintained in culture for further infections. The retroviral solution was used for spin infection of MT cells by centrifuging 45 min at 1800 rpm at 37°C. In total, four spin infections were performed over two days. Positively infected cells were selected with puromycin (Serva) or blasticidin (GIBCO) and, eventually, GFP positivity was analyzed using a BD FACS Calibur
Yuan Z., VanderWielen B.D., Giaimo B.D., Pan L., Collins C.E., Turkiewicz A., Hein K., Oswald F., Borggrefe T, & Kovall R.A. (2019). Structural and Functional Studies of the RBPJ-SHARP Complex Reveal a Conserved Corepressor Binding Site. Cell reports, 26(4), 845-854.e6.
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