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Exact(11)
For the GST pull-down assays, bound proteins were resolved in an 8% SDS-PAGE polyacrylamide gel and transferred in the same abovementioned way.
Specifically bound proteins were resolved by SDS-PAGE and visualized by Silver staining.
Bound proteins were resolved by PAGE, transferred onto PVDF membranes, and analyzed by immunoblotting.
Bound proteins were resolved by SDS-PAGE and blotted onto nitrocellulose membranes.
The beads were washed three times with IP-buffer and bound proteins were resolved by 10% SDS-PAGE.
Immunoprecipitates were washed three times with RIPA buffer and the bound proteins were resolved in 10% SDS-PAGE gels for immunoblot analysis with the relevant antibodies.
Similar(49)
The bound fraction was washed three times with ice-cold 1× binding buffer and then solubilized in 2XSB; 75% of the bound and 37.5% of the unbound proteins were resolved by SDS PAGE.
Bound gephyrins were released by boiling in SDS‐loading buffer, and proteins were resolved on a 6% SDS PAGE.
Proteins were resolved by SDS-PAGE.
Eluted proteins were resolved by SDS-PAGE.
Bound proteins were eluted, resolved on an SDS PAGE gel and proteins within visibly stained gel bands were excised and identified by MS. Using this approach, it was shown that the NuRD complex associates with unmodified histone H3 peptides and is prevented from binding by trimethylation at lysine 4 [ 84].
More suggestions(13)
bound proteins were dissolved
bound proteins were eluted
bound proteins were solubilized
bound proteins were separated
bound proteins were detected
bound proteins were analyzed
bound proteins were visualized
bound complexes were resolved
bound proteins were released
bound proteins were analysed
bound proteins were subjected
bound fractions were resolved
bound proteins were washed
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