Figure 3
We pulled down biotinylated tubulins from HEK293T cells expressing either ‘single’ or ‘dual’ tubulin constructs. TAPs were co-precipitated and identified using mass spectrometry. The ‘single’ approach yielded 42 potential TAPs, whereas the ‘dual’ approach yielded 328 candidate TAPs (note that these numbers were obtained after filtering of the original mass spectrometry data). Here, we compare co-precipitation of different classes of proteins (V: various proteins of this class are present in the dataset, +/-: only few proteins of this class are present in the dataset, - : no proteins of this class are present in the dataset).
Comparison of mass spectrometry experiments

We pulled down biotinylated tubulins from HEK293T cells expressing either ‘single’ or ‘dual’ tubulin constructs. TAPs were co-precipitated and identified using mass spectrometry. The ‘single’ approach yielded 42 potential TAPs, whereas the ‘dual’ approach yielded 328 candidate TAPs (note that these numbers were obtained after filtering of the original mass spectrometry data). Here, we compare co-precipitation of different classes of proteins (V: various proteins of this class are present in the dataset, +/-: only few proteins of this class are present in the dataset, - : no proteins of this class are present in the dataset).

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