Nuclear samples were precipitated via the acetone precipitation [59] method to increase their concentrations so that 75 µg of nuclear protein could be loaded in each well.
Pooled samples were precipitated using the ProteoExtract Protein Precipitation Kit (Calbiochem, Germany), according to the manufacturer's protocol.
Samples were precipitated by methanol/chloroform.
The blood samples were precipitated with methanol, centrifuged, from which the supernatant was separated on UPLC with C18 column and eluted in gradient with acetonitrile and Milli-Q water both containing 0.1% formic acid (FA).
To reveal the presence and effect of catalyst residues, the crude product PTMS samples were precipitated in methanol from their chloroform solution, and were further refluxed in an acid solution to selectively hydrolyse the weak metal alkoxide moieties formed.
The samples were precipitated with ethanol and glycogen (Thermo Scientific, R0551) and analyzed by 6% urea-PAGE.
Next, using a magnet with an intensity of 8 T, nanoparticles inside the samples were precipitated and samples filtered using a syringe equipped with a 0.22 μm filter.
The as-prepared QD samples were precipitated by 2-propanol and dried in a vacuum oven for X-ray diffraction (XRD) characterization.
Samples were precipitated by addition of acetone and dried in vacuum prior to characterization by X-ray diffration (XRD), Fourier-transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and transmission electron microscopy (TEM).
After end-labeling, samples were precipitated as described above and dissolved in NEB4 buffer supplemented with BSA for Bsp1286I digestion (New England Biolabs).
Briefly, samples were precipitated with an equal volume of 5% trichloroacetic acid, centrifuged at 3000 g for 5 mins, and the supernatants used for the analysis.
