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Approx. 25 µl of protein extract from each sample was loaded into wells on gel plates containing trypsin (Sigma-Aldrich) dissolved in plant agar.
Samples were then randomized, and 10 μl from each sample was loaded into a 96 well plate for genotyping.
Protein from each sample was loaded into a 10%% sodium dodecyl sulfate (SDS -polyacrylamide electrophoreSDS -polyacrylamiderrelectrophoresisllulose membrane (Amersham Biosciences, Piscataway, NJ).
Protein (30 µg) from each sample was loaded into a gradient gel and run at constant current until protein markers had adequately separated.
A volume of 20 μl from each sample was loaded into the chromatographic system consisting of a C18 preconcentration cartridge (Agilent Technologies) connected to a 15-cm-long, 100 μm i.d.
A total of 5 μg of protein from each sample was loaded into the gel and the proteins were separated by electrophoresis at 100 V for 2 h 30 min.
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Normalized bead intensity data obtained for each sample were loaded into the Illumina BeadStudio™ software version 3.1.3.0, which calculated CNV data from Intensity and B allele frequency.
A total of 30 µg of protein (from myocardial tissue) or 30 µL of protein (from isolated cardiomyocytes) of each sample was loaded into 12.5% acrylamide gels.
A total volume of 100 μl of each sample was loaded into the eight loading ports on the TLDA card (2 ports for each sample, 4 samples total on one card).
Equal concentrations of protein from each sample were loaded into a 10% acrylamide gel and separated by SDS-PAGE.
For this, each complete sample was loaded into three wells.
More suggestions(15)
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