Figure S1.
Purified proteins used in dynein motility assays. (A) Coomassie Blue-stained SDS-PAGE of the purified proteins. The expected molecular weight (kDa) of each purified protein is indicated. For dynein and dynactin complexes, the size and name of each subunit are specified. Western blots (dashed frames) were performed to detect the smallest dynein subunits (not visible on SDS-PAGE) and verify the identity of some dynactin SDS-PAGE bands. (B) Analysis of the oligomeric state of each purified protein by mass photometry. The molecular weight, with the associated standard deviation (σ), of the most abundant species present in each sample is indicated in the mass histograms. The symmetric parts of the histograms around mass 0 kDa represent the background signal of the buffer. For AF647-NuMAN-term, the 162 kDa peak may represent the oligomerized state of a minor contaminant of 80–85 kDa. Source data are available for this figure: SourceData FS1.

Purified proteins used in dynein motility assays. (A) Coomassie Blue-stained SDS-PAGE of the purified proteins. The expected molecular weight (kDa) of each purified protein is indicated. For dynein and dynactin complexes, the size and name of each subunit are specified. Western blots (dashed frames) were performed to detect the smallest dynein subunits (not visible on SDS-PAGE) and verify the identity of some dynactin SDS-PAGE bands. (B) Analysis of the oligomeric state of each purified protein by mass photometry. The molecular weight, with the associated standard deviation (σ), of the most abundant species present in each sample is indicated in the mass histograms. The symmetric parts of the histograms around mass 0 kDa represent the background signal of the buffer. For AF647-NuMAN-term, the 162 kDa peak may represent the oligomerized state of a minor contaminant of 80–85 kDa. Source data are available for this figure: SourceData FS1.

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal