The EMSA was conducted using 50 nM of 5’ 6-Fluorescein (5’ 6-FAM) pT labelled DNA (hybridized or not with the complementary non-fluorescent DNA strain to form ssDNA and dsDNA) from IDT. LMNG was used as a detergent for TraE, while Triton X-100 was used for TraD. Proteins were diluted in 10 mM Tris pH 9.5, 150 mM NaCl, 10% glycerol, 5x detergent CMC and incubated with DNA for 30 min at 4 °C. Samples were loaded on a 0.5% agarose gel and run in the running buffer: 0.5X Tris-Borate-EDTA (TBE) pH 9.5, 150 mM NaCl, 5% glycerol, 5x detergent CMC at 90 V, 4 °C for 2 h. Agarose gels were prepared by solubilizing agarose with the running buffer, and gel revelation was acquired using a Fluorescein filter from the ChemiDoc MP imaging system. For BAR-072 inhibition experiments, all solutions and gels were supplemented with 10% DMSO.
Mp imaging system
Manufactured by Bio-Rad
57 citations
Sourced in United States
About the product
The MP Imaging System is a versatile instrument designed for high-resolution, quantitative imaging of molecular interactions and cellular processes. The system utilizes advanced optics and sensitive detectors to capture detailed images of fluorescent samples. The core function of the MP Imaging System is to provide researchers with a powerful tool for visualizing and analyzing complex biological phenomena.
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Check compatibility
57 protocols using «mp imaging system»
1
EMSA Assay for TraE and TraD
2
HA Hydrogel-Mediated DiD Release and In Vivo Tracking
DiD release from the HA hydrogel was detected in vitro using MicroplateReader, with excitation wavelength of 644 nm and emission wavelength of 665 nm. The excitation wavelength for Cy5 is 654 nm and emission wavelength is 670 nm. The 0.5 mL HA (containing 0.1 mg DiD and 0.2 mg HA in 0.9% NaCl solution) was added to a 1.5 mL eppendorf tube and 0.5 mL 0.9% NaCl buffer with or without 5 unit mL−1 proteinase K was added at 37°C. At indicated time points, 10 µL sample was mixed with 190 µL 0.9% NaCl buffer, which was stored in −20°C and measured at the same time. For in vivo detection, 100 µL HA‐DiD (1 µm ) or free DiD (1 µm ), RTD‐Cy5 (0.5 µm ) or HA@RTD‐Cy5 (0.5 µm ) was subcutaneously injected in mice and the signal was detected by the ChemiDoc MP Imaging System at different time points.
3
Biocomposite Materials Synthesis and Characterization
Spore suspensions (OD600 = 0.5) were prepared in distilled water and subsequently lyophilized. 12.5 mg PCL (in 3 w/v% DCM) was mixed with lyophilized spore powder from 1 mL of the spore suspension. 10 s vortexing was applied to ensure a homogeneous mixing of spore particles. 100 μL of the mixed solutions was directly drop-cast on the glass substrate to form biocomposite materials. For mechanical testing, 200 μL of the mixed solutions was directly drop-cast into a dog-bone-shape mold (WLH, PTFE). The residual solvents were evaporated under ambient temperature and pressure overnight. For tensile tests, the dog-bone-shaped materials were loaded on the Instron (3365 Universal Testing System) and pulled with a speed of 10 mm min-1. For spontaneous degradation tests, circle-shaped biocomposite materials were immersed into 100 mM Tris-HCl buffer with agitation (42 °C, 800 rpm). The remaining materials were collected as much as possible at each time point, washed with 50 mL distilled water for 10 seconds, imaged under Chemidoc MP imaging system, and dried under an ambient environment before measuring crystallinity and SEM imaging.
4
Spheroid Diameter Measurements and Western Blot
The diameters of the spheroids cultured as specified in Section 4.5.2 were measured at the end of the 4th day. Spheroids of equal size, reaching a diameter of 400 µm, were selected and transferred to the wells of another sterile 96-well cell culture plate. Concentrations of IC50 values determined in spheroid cultures of MVB1, MVB2, and rapamycin were prepared in 200 µL of medium and added to the wells. Twenty-four hours of incubation were provided. After applying the western blot protocol to the collected spheroids, as specified in Section 4.6.1 , the membranes were incubated with ECL Western imaging solution for 5 min and then imaged using automatic exposure with the Chemidoc MP imaging system. The recorded images were analyzed with the Image J 1.4.3.67 program.
5
Optimized Tdp1 Activity Assay in Zebrafish
The TDP1 activity assay optimized for detecting Tdp1 activity in zebrafish embryos was performed as described previously (Anticevic et al., 2023 (link)). In brief, 600 ng of embryo lysates were incubated with a Tdp1 oligonucleotide substrate (Table 5 ), containing a tyrosine at the 3′ end of the DNA and Cy5 at the 5′end. Active Tdp1 removes the tyrosine from the 3′ end, causing a shift in the size of the substrate. 2 dpf tdp1−/− mutants and WT embryos, with or without transient overexpression of tdp2a and tdp2b mRNA, were deyolked and homogenized for 10 s in 100 μL of lysis buffer (200 mM Hepes, 40 mM NaCl, 2 mM MgCl2, 0.5% Triton X-100 with protease inhibitors), followed by incubation on ice for 30 min. Next, the supernatant protein solution (600 ng) was incubated with 2.5 µM labeled oligonucleotide substrate in assay activity buffer (25 mM Hepes (pH 8.0), 130 mM KCl, and 1 mM dithiothreitol (DTT)) in a final reaction mixture of 10 μL. The reaction proceeded at 37°C for 1 h, after which loading buffer was added, and the mixture was boiled at 95°C for 5 min. All samples were loaded onto a pre-run 20% homemade urea gel and run at a constant voltage (120 V) for 2 h. The resulting oligonucleotide products were visualized using the ChemiDoc MP Imaging System to detect Cy5 fluorescence.
Top 5 most cited protocols using «mp imaging system»
1
Quantification of Dystrophin Isoforms
Mouse muscle lysates were prepared using 4 M urea lysis buffer (pH 6.8); 150 μL of lysis buffer was added to ten sections of 20-μm-thick tissue. Tissue was lysed using a metal bead (2 min at 30 Hz, TissueLyser II; Qiagen). The solution was incubated at room temperature for 30 min prior to a second lysis step (1 min at 30 Hz, TissueLyser II). The solution was incubated again at room temperature for 30 min. The solution was then centrifuged at 14,000 × g for 20 min and supernatant extracted for analysis. Protein was quantified using a Bio-Rad DC assay kit (catalog #5000112). A calibration curve was made by spiking in WT dystrophin from C57Bl/6 mice into dystrophin-null lysate from a Dup2Del18-41 mouse. All samples were mixed with 4× Laemmli buffer prior to incubation at 95°C for 5 min. Thirty micrograms of total protein was loaded on a precast 3%–8% tri-acetate gel and ran for 1 h at 80 V followed by 2 h at 120 V. Gels were transferred overnight at 4°C, constant 55 mA onto a 0.45-μm polyvinylidene fluoride membrane. Membranes were cut at 150 kDa marker for probing. The top halves of membranes were probed using a polyclonal rabbit antibody specific to the C terminus of dystrophin (ab15277, 1:200 or ab154168, 1:1,000; Abcam). Membranes were then washed four times for 5 min in 0.1% Tween 20 containing PBS (PBST). Secondary antibody goat anti-rabbit HRP (1:5,000) for 1 h at room temperature followed by five 5-min washes with PBST and one 5-min wash with PBS. Membranes were incubated with 2 mL of ECL reagent (Thermo Scientific, #34580) prior to visualization on a Chemidoc MP Imaging System. Dystrophin signals were quantified using Image Lab software (version 6.0.0 build 25). Individual mouse samples were quantified using a linear regression curve fitted to a calibration curve on each gel. The full-length (427 kDa) and IRES-driven (413 kDa) dystrophin isoforms could not be differentiated on the western blots.
Corresponding organizations : Nationwide Children's Hospital, The Ohio State University, University of Utah
2
Fluorescent Labeling of Proteomes
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Corresponding organizations : University of Virginia, Virginia Commonwealth University
3
Immunoblotting of Phosphorylated Signaling Proteins
Cell lysates were separated via centrifugation at 100 000 × g for 45 min at 4 °C. Proteins separated by SDS-PAGE (4–20% polyacrylamide, TGX Stain-Free MIDI Gel). Gel transfers were performed using the Bio-Rad Trans-Blot Turbo RTA Midi Nitrocellulose Transfer Kit with a Bio-Rad Trans-Blot Turbo Transfer System. After incubation with 5% milk in TBST (1.5 M NaCl, 0.25 M Tris pH 7.4, 0.1% Tween 20, in ultrapure water (ddH2O)) for 1 h. The membrane was incubated with primary antibody p-RSK (1 : 1000), or p-ERK1/2 (1 : 1000) for 12 h at 4 °C. After the primary antibody incubation, membranes were washed 5 times for 5 min with TBST and incubated with secondary antibody (1 : 10 000) for 2 h at 25 °C. The membrane was washed 5 times for 5 min with TBST and imaged with a Chemidoc MP Imaging system.
Corresponding organizations : University of Virginia, Charlottesville Medical Research
4
Subcellular Localization of TOPLESS and SIX Effectors
Agrobacterium tumefaciens strain GV3101 was transformed with pDEST‐VYNE(R)GW::TPL1 to ‐TPL5, pDEST‐SCYCE(R)GW::SIX3 or ‐SIX8 and pGWB454::NLS‐mCherry. Equal amounts of A. tumefaciens transformed with (1) pDEST‐VYNE(R)GW containing a specific TOPLESS homologue, (2) pDEST‐SCYCE(R)GW containing either SIX3 or SIX8 and (3) pGWB454::NLS‐mCherry were mixed to an OD600 of 1.0 and infiltrated in the same leaf. Leaves were harvested at 24 hpi for fluorescence imaging of epidermal cells (LSM510, Zeiss, 40×/1.2 and 20×/0.75 objectives). The fluorophores were excited at 488 nm (GFP) or 543 nm (RFP) and emission was detected using a band‐pass filter (505–530 nm or 585–615 nm, respectively). The GFP intensity of the resulting images was analysed using an ImageJ script (Data S2 ). The data were log10 normalized before statistical analysis. Accumulation of the c‐myc‐tagged TPLs and HA‐tagged SIX8 and SIX3 effectors was assessed by immunoblotting. Proteins were extracted from four leaf discs (4 mm) as described (Cao et al., 2018 (link)). To detect the fusions proteins, anti c‐myc (α‐myc, 9E10, Roche 11667149001, 1 : 1000 dilution) and anti‐HA monoclonal antibodies (α‐HA 3F10, Roche 11867423001, 1 : 2000 dilution) were used. In both cases, a secondary goat‐anti‐mouse antibody (Pierce 31430) was used in a 1 : 5000 dilution. Chemiluminescence was detected using a Chemidoc MP imaging system.
Corresponding organizations : Netherlands Institute for Neuroscience, University of Amsterdam, Zero to Three
5
Proteome Enrichment and Labeling Protocol
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