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Chemidoc mp visualization system

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The ChemiDoc MP Visualization System is a compact and versatile imaging system designed for a wide range of applications in life science research laboratories. It is capable of capturing high-quality images of chemiluminescent, colorimetric, and fluorescent samples.

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Lab products found in correlation

Supersignal west dura kit, by Thermo Fisher Scientific (4 mentions) Dc protein assay, by Bio-Rad (4 mentions) Image lab, by Bio-Rad (4 mentions) Criterion tgx, by Bio-Rad (3 mentions) Criterion tgx tris glycine extended stain free page gels, by Bio-Rad (2 mentions) Stain free page gels, by Bio-Rad (2 mentions) Ecl prime western blotting system, by Cytiva (1 mentions) Mitochondria isolation kit for tissue, by Thermo Fisher Scientific (1 mentions)

8 protocols using chemidoc mp visualization system

1

Western Blot Analysis of Mitochondrial Proteins

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Mitochondrial fractions were obtained using the Mitochondria Isolation Kit for Tissue (89801, ThermoFisher Scientific, Waltham, MA). Protein concentrations were measured with the DC protein assay (Bio-Rad Laboratories, Hercules, CA, USA). Equal amounts of protein were loaded into lanes of Criterion TGX (Tris–Glycine eXtended) Stain-Free PAGE gels (Bio-Rad Laboratories, Hercules, CA, USA. The gels were electrophoresed and activated using a ChemiDoc MP Visualization System (Bio-Rad Laboratories, Hercules, CA, USA). The protein was then transferred to a PVDF membrane. The membranes were then imaged using a ChemiDoc MP Visualization System to obtain an assessment of proper transfer and to obtain total protein loads. The membranes were then blocked and probed with primary antibodies overnight at 4 °C. Immunoblots were next processed with secondary antibodies (Cell Signaling) for 1 h at room temperature. Immunoblots were then probed with a Super Signal West Dura kit (Thermo Fisher Scientific) to visualize signal, followed by visualization using a ChemiDoc MP Visualization System (Bio-Rad Laboratories, Hercules, CA, USA). Data were analyzed using Image Lab (Bio-Rad Laboratories, Hercules, CA, USA)58 (link). Uncropped images of immunoblots are depicted in Supplemental Figs. 1–5.
Pantner Y., Polavarapu R., Chin L.S., Li L., Shimizu Y, & Calvert J.W. (2021). DJ-1 attenuates the glycation of mitochondrial complex I and complex III in the post-ischemic heart. Scientific Reports, 11, 19408.
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2

Western Blot Analysis of Protein Samples

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Whole cell fractions were obtained as previously described.23 Protein concentrations were measured with the DC protein assay (Bio‐Rad Laboratories, Hercules, CA). Equal amounts of protein were loaded into lanes of CriterionTGX (Tris‐Glycine eXtended) Stain‐Free PAGE gels (BioRad). The gels were electrophoresed and activated using a ChemiDoc MP Visualization System (BioRad). The protein was then transferred to a polyvinylidene difluoride membrane. The membranes were then imaged using a ChemiDoc MP Visualization System to obtain an assessment of proper transfer and to obtain total protein loads. The membranes were then blocked and probed with primary antibodies overnight at 4°C. Immunoblots were next processed with secondary antibodies (Cell Signaling) for 1 hour at room temperature. Immunoblots were then probed with a Super Signal West Dura kit (Thermo Fisher Scientific) to visualize signal, followed by visualization using a ChemiDoc MP Visualization System (BioRad). Data were analyzed using Image Lab (BioRad). The total protein images were used as loading controls. For each protein of interest, the portion of the protein load image corresponding to the molecular weight of the protein of interest was used as the loading control.23
Shimizu Y., Nicholson C.K., Polavarapu R., Pantner Y., Husain A., Naqvi N., Chin L., Li L, & Calvert J.W. (2020). Role of DJ‐1 in Modulating Glycative Stress in Heart Failure. Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 9(4), e014691.
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3

Immunoblotting Protein Quantification Protocol

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Whole cell fractions were obtained, as previously described.22 Protein concentrations were measured with the DC protein assay (Bio‐Rad Laboratories, Hercules, CA). Equal amounts of protein were loaded into lanes of Criterion TGX (Tris‐Glycine eXtended) Stain‐Free PAGE gels (BioRad). The gels were electrophoresed and activated using a ChemiDoc MP Visualization System (BioRad). The protein was then transferred to a polyvinylidene difluoride membrane. The membranes were then imaged using a ChemiDoc MP Visualization System to obtain an assessment of proper transfer and to obtain total protein loads. The membranes were then blocked and probed with primary antibodies overnight at 4°C. Immunoblots were next processed with secondary antibodies (Cell Signaling) for 1 hour at room temperature. Immunoblots were then probed with a Super Signal West Dura kit (Thermo Fisher Scientific) to visualize signal, followed by visualization using a ChemiDoc MP Visualization System (BioRad). Data were analyzed using Image Lab (BioRad). The total protein images were used as loading controls. For each protein of interest, the portion of the protein load image corresponding to the molecular weight of the protein of interest was used as the loading control.23
Shimizu Y., Polavarapu R., Eskla K., Pantner Y., Nicholson C.K., Ishii M., Brunnhoelzl D., Mauria R., Husain A., Naqvi N., Murohara T, & Calvert J.W. (2018). Impact of Lymphangiogenesis on Cardiac Remodeling After Ischemia and Reperfusion Injury. Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 7(19), e009565.
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4

Western Blot Analysis of Protein Fractions

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Whole cell, cytosolic, and nuclear fractions were obtained from heart homogenates as previously described [21 (link)]. Protein concentrations were measured with the DC protein assay (Bio-Rad Laboratories, Hercules, CA, USA). Equal amounts of protein were loaded into lanes of Criterion™ TGX (Tris-Glycine eXtended) Stain-Free PAGE gels (BioRad). The gels were electrophoresed and activated using a ChemiDoc MP Visualization System (BioRad). The protein was then transferred to a PVDF membrane. The membranes were then imaged using a ChemiDoc MP Visualization System to obtain an assessment of proper transfer and to obtain total protein loads. The membranes were then blocked and probed with primary antibodies (Supplemental Table 2) overnight at 4 °C. Immunoblots were next processed with secondary antibodies (Cell Signaling) for 1 hour at room temperature. Immunoblots were then probed with a Super Signal West Dura kit (Thermo Fisher Scientific) to visualize signal, followed by visualization using a ChemiDoc MP Visualization System (BioRad). Data was analyzed using Image Lab (BioRad). The total protein images were used as loading controls. For each protein of interest, the portion of the protein load image corresponding to the molecular weight of the protein of interest was used as the loading control [16 (link)].
Shimizu Y., Polavarapu R., Eskla K.L., Nicholson C.K., Koczor C.A., Wang R., Lewis W., Shiva S., Lefer D.J, & Calvert J.W. (2018). Hydrogen Sulfide Regulates Cardiac Mitochondrial Biogenesis via the Activation of AMPK. Journal of molecular and cellular cardiology, 116, 29-40.
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5

CLOCK Protein Expression Analysis

Cited 3 times
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Heart samples from each group at one month were homogenized and lysates at light phase or at different time point were prepared as previously described. H9c2 cells were homogenized immediately after 48 h of transfection with siRNA targeting CLOCK5 (link). Equal amounts of protein were subjected to CriterionTGX (Tris–Glycine extended) Stain-Free PAGE gels (BioRad) and activated using a ChemiDoc MP Visualization System (BioRad). The protein was then transferred to PVDF membranes as previously described49 (link),56 (link). Those membranes were then imaged to obtain total protein loadings. The membranes were blocked and probed with the targeted primary antibodies, followed by incubation with secondary antibodies. The protein signal was detected using an ECL Prime Western Blotting System (Cytiva). Protein expression was analyzed by measuring band intensities using Image J software49 (link). Average photoperiod quantification of CLOCK protein expression was normalized to total protein. The antibodies are described in the Supplemental Materials.
Che Y., Shimizu Y., Hayashi T., Suzuki J., Pu Z., Tsuzuki K., Narita S., Shibata R, & Murohara T. (2024). Chronic circadian rhythm disorder induces heart failure with preserved ejection fraction-like phenotype through the Clock-sGC-cGMP-PKG1 signaling pathway. Scientific Reports, 14, 10777.
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6

Unwinding of RNA G-Quadruplexes by DExH Helicases

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The rG4 unwinding assays were performed using gel shift according to the procedure described in a published work in three independent repetitions (41 (link)). Briefly, different concentrations of purified DExH1 and DExH15 were mixed with 160 nM rG4 substrates in 25 mM Tris–HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 2 U/μl RNase inhibitor, 10% glycerol, and 1 mM DTT. The mixture was incubated for 10 min at 37 °C. Then, one equal volume of 4 mM ATP was added along with 1.6 μM traps to initiate reactions and incubated for 30 min at 37 °C. Then 5× stop buffer (125 mM EDTA and 50% glycerol (v/v)) and proteinase K (final concentration of 2 mg/ml) were added sequentially. After waiting for 10 min at 37 °C, the reaction products were electrophoresed on a 12% native PAGE. Finally, the gels were imaged using the Cy3 channel on a ChemiDoc MP Visualization System (BioRad) and analyzed in ImageJ (National Institutes of Health).
Wang L., Xu Y.P., Bai D., Shan S.W., Xie J., Li Y, & Wu W.Q. (2022). Insights into the structural dynamics and helicase-catalyzed unfolding of plant RNA G-quadruplexes. The Journal of Biological Chemistry, 298(8), 102165.
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7

Quantifying hnRNP K-RNA Interactions

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Different concentrations of hnRNP K were mixed with 80 nM fluorescently labeled Py25′ in reaction buffer (pH 5.8). The mixture was electrophoresed on an 8% native PAGE after being incubated for 20 min at 22 °C. The gels were run in TAE buffer containing 200 mM KCl and imaged on a ChemiDoc MP Visualization System (BioRad); the images were analyzed in ImageJ (National Institutes of Health).
Wu W.Q., Zhang X., Bai D., Shan S.W, & Guo L.J. (2022). Mechanistic insights into poly(C)-binding protein hnRNP K resolving i-motif DNA secondary structures. The Journal of Biological Chemistry, 298(12), 102670.
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8

Vacuolar Lipid Extraction and Characterization

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Lipids were extracted from purified DKY6281 and dgk1Δ vacuoles (200 μg protein content) by the method of Bligh and Dyer then dried overnight under vacuum.87 (link) Purified lipids were resuspended in chloroform:methanol (2:1) before being resolved by neutral lipid thin-layer chromatography as previously described.88 (link) Briefly, Whatman Partisil® LK6D Silica Gel Plates (60 Å) were pre-washed with methanol/ethyl acetate (6:4) for 30 minutes. Individual channels were loaded with the indicated amount of diacylglycerol standard (Avanti Lipids) or vacuolar lipids. Plates were run twice with CH2Cl2/ethyl acetate/acetone (80:16:4) to 40 and 55 mm then hexanes/ethyl acetate to 68 mm (90:10), 80 mm (95:5), and 90 mm (100:0). Plates were then sprayed with a solution of 10% copper (II) sulfate in 8% phosphoric acid and dried for 10 minutes before charring at 145º C for 10 minutes. Imaging of plates was performed using a BioRad ChemiDoc™ MP Visualization System (605/50 filter, Green Epi illumination). Densitometry values were measured using Image Lab 4.0.1 software.
Miner G.E., Starr M.L., Hurst L.R, & Fratti R.A. (2017). Deleting the DAG Kinase Dgk1 Augments Yeast Vacuole Fusion Through In-creased Ypt7 Activity and Altered Membrane Fluidity. Traffic (Copenhagen, Denmark), 18(5), 315-329.
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