Myotubes (differentiated for 7 days) were placed in serum-free DMEM containing 1% BSA for 3 h. After incubation, the myotubes were treated with AICAR (1 mM), WH, or vehicle (0.1% DMSO) for the indicated time or condition. After treatment, the cells were lysed [15] (link). Aliquots of supernatant were boiled in Laemmli sample buffer for 5 min [16] (link). The samples (25 μg protein) were then resolved in SDS–PAGE, transferred onto nitrocellulose membranes, and the blots were probed with various antibodies for 16 h at 4 °C. The membranes were then reacted with horseradish peroxidase-conjugated anti-rabbit or mouse IgG antibody, the immunoreactivity was visualized using ECL reagent (GE Healthcare Bioscience, Tokyo, Japan), and the relative density was evaluated with Multi Gauge Ver. 3.0 Densitograph Software (Fuji Film, Tokyo, Japan). The experiments were performed in triplicate and representative results are shown.
Multi gauge ver 3.0 densitograph software
Manufactured by Fujifilm
Sourced in Japan
The Multi Gauge Ver. 3.0 Densitograph Software is a densitometry tool developed by Fujifilm. It is designed to measure and analyze the optical density of photographic and printed materials. The software provides detailed information about the density levels across the measured sample.
Automatically generated - may contain errors
Lab products found in correlation
2 protocols using multi gauge ver 3.0 densitograph software
1
AICAR-Induced Myotube Signaling Analysis
2
Western Blot Analysis of GLUTag Cells
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The medium of cultured GLUTag cells was replaced with serum-free Dulbecco’s modified Eagle’s medium containing 1% BSA for 3 h. After incubation, the cells were treated with vehicle (0.1% DMSO) or D3R for the indicated time periods and conditions and then lysed [28 (link)]. Supernatant aliquots were treated with Laemmli sample buffer for 5 min at 100°C [29 (link)], and the samples (20 μg protein) were separated by SDS-PAGE. After electrophoresis, proteins were transblotted onto nitrocellulose membranes and probed with various primary antibodies for 16 h at 4°C. The proteins were then reacted with horseradish peroxidase-conjugated anti-rabbit antibody, and immunoreactivity was visualized using Pierce Western Blotting Substrate (Thermo Fisher Scientific, Yokohama, Japan). The relative density of the stained proteins was evaluated using Multi Gauge Ver 3.0 Densitograph Software (Fuji Film, Tokyo, Japan).
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