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After washing and elution in SDS-containing loading buffer, proteins were separated by SDS-PAGE.
Sciatic nerves from untreated adult mice were homogenized in lysis buffer, proteins were separated by SDS-PAGE and transferred onto nitrocellulose for immunoblot analyses.
Ten tissue specimens, three from wild-type, three from C7-hypomorphic, and four from losartan-treated C7-hypomorphic mice, were lysed in SDS buffer, proteins were separated by SDS PAGE and digested in-gel, and the resulting peptide fractions were analyzed by label-free, quantitative mass spectrometry.
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After washing five times in lysis buffer, the beads were boiled in Laemmli buffer, the proteins were separated by SDS-PAGE, followed by immunoblotting as described previously [69].
After incubation at room temperature for 30 min the reaction was stopped by adding protein loading buffer and proteins were separated on SDS-PAGE gels.
HIS6SMN/GST-Gemin2 heterodimers were cleaved with Calpain1, as described above, and samples were mixed with 5X SDS sample buffer and proteins were separated by SDS-PAGE.
After 5 washes in the lysis buffer, bound proteins were separated by SDS-PAGE analyzedyzed by Western blotting using anti-CD4 H370 and anti-GFP antibodies.
Following incubation, cells were harvested and particulate and cytosolic fractions were obtained using the M-Per protein extraction buffer, and proteins were separated by SDS-PAGE followed by western blotting as described above using anti-HA antibody.
Subsequently, the beads were precipitated using a magnetic rack and washed in 10 mM HEPES (pH 7.35) than boiled for 5 min in Laemmli sample buffer, and proteins were separated by SDS PAGE.
Each pellet was resuspended in sample buffer and proteins were separated by gel electrophoresis.
hTERT-RPE1 cells were lysed in SDS sample buffer, and proteins were separated by SDS-PAGE on 4 12% gel.
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