Sentence examples for bound materials were eluted from inspiring English sources

The bound materials were eluted by a buffer containing FLAG peptide (0.2 mg/ml).

The bound materials were eluted using 0.2 mg/ml 3X FLAG peptide (Sigma) in 25 mM Hepes, pH 7.2, 115 mM potassium acetate, 5 mM sodium acetate, 2.5 mM magnesium acetate.

The serum was initially applied to a TrpE-hMGMT-1-coupled column; their bound materials were eluted at pH 2.3 and dialysed against 10 m M Tris-HCl (pH 7.4) and 150 m M NaCl.

The extract was applied on Q Sepharose FF pre-equilibrated with buffer A (50 mM Tris-HCl, pH 7.4), and bound materials were eluted by running a NaCl-gradient (0→1 M) in buffer A. Various nuclease activities were detected after separation, and the double-strand (ds) specific activity addressed in this report eluted at 0.4 M NaCl.

Beads were pelleted for 30 sec at 2000 g in a microcentrifuge and bound material was eluted with 25 µl of 2x SDS sample buffer, heated for 5 min, and frozen at −20°C.

The beads were washed three times with 150 μL of binding buffer, and bound material was eluted by boiling in SDS loading buffer.

Specifically bound material was eluted with 300 mM NaCl, 500 mM imidazole, 100 mM Tris (pH 7.4) and submitted to non-reducing SDS-PAGE.

After extensive washes, bound material was eluted using RNase H (New England Biolabs (NEB), UK) for 30 min at room temperature.

Non-bound material was removed by washing the beads four times with BN-lysis buffer, and bound material was eluted by competition with synthetic myc peptide (Sigma) for 2 h at 4 °C.

Beads were washed again and bound material was eluted from beads with 50  μl SDS-PAGE sample buffer at 50 °C, using microSpin columns (Promega, San Luis Obispo, CA, USA) at 5000 × g for 5 min.

The beads were washed four times with binding buffer, and bound material was eluted by denaturation in SDS loading buffer and detected by western blotting with anti-FLAG antibody.