Sentence examples for buffer samples were eluted from inspiring English sources

After several washes with NETN buffer, samples were eluted by boiling in Laemmli sample buffer including β-ME and subjected to SDS-PAGE.

After three washing steps in NET buffer, samples were eluted in Laemmli loading buffer [62.5 mM Tris/HCl (pH 6.8), 2% (w/v) SDS, 10% (v/v) glycerol, 0.1% 2-mercaptoethanol and 0.0005% Bromophenol Blue] and the eluted proteins were separated by SDS/PAGE (10% gel) for Western blotting.

After the beads were washed three times with 1 ml of RIPA buffer, samples were eluted in 100 μl of reducing SDS sample buffer at 95°C for 5 min. Aliquots (20 μl) of each sample were subjected to SDS PAGE and immunoblotting with anti-Nyv1p antibody.

The column was equilibrated in buffer C. Samples were eluted isocratically in buffer C, monitoring at 220 and 280 nm.

After a washing step (4 CV) in the same buffer, the samples were eluted applying a linear imidazole gradient (25 250 mM over 18 CV).

After three washes in lysis buffer containing RNAsin, samples were eluted in SDS sample buffer (10 min at 98°C).

The resins were washed three times with lysis/binding/washing buffer and the samples were eluted by adding 50 μl of 2X SDS sample buffer and boiling at 95°C for 5 minutes.

For co-immunoprecipitation experiments with purified proteins, the immunoprecipitated samples were eluted with elution buffer (Thermal Scientific, USA) and neutralized with Tris buffer (pH 9.0).

Immunoprecipitated chromatin samples were eluted in elution buffer (1% SDS, 100 mM NaHCO3) for 15 min at 65°C and reverse cross-linked overnight at 65°C with 200 mM NaCl.

The next day, the beads were washed 3 times with Lysis Buffer without detergent and samples were eluted with 70 µl of 1× FLAG-peptide solution (Sigma, 100 200 µg/ml) or HA-peptide solution (Sigma, 100 µg/ml), respectively, in 1× Tris-buffered saline (150 mM NaCl, 10 mM Tris-HCl pH 7.0).

After washing, using buffers A and B samples were eluted using aliquots of 0.5% NH4OH.