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After washing, the binding sequences were eluted by heating, and the recovered ssDNA was used to perform negative selection using HCT 116.
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DNA not specific to these regions were washed off and targeted DNA sequences were eluted and amplified by emulsion PCR.
The sample was washed and the bead-binding complexes were eluted with elution buffer [ 48].
After washing with binding buffer (PIERCE), the binding proteins were eluted with 0.1 M glycine-HCl (pH 2.2).
The specific Tpm1 binding proteins were eluted using different buffers: 0.5 M KCl or 3 M urea in HEK buffer.
Binding proteins were eluted with a salt gradient of 0 - 1 M NaCl.
The non-specific binding proteins were eluted with 10 CV of PBS buffer.
The beads were then proper washed and the binding proteins were eluted by 1× SDS-PAGE sample loading dye.
Choline-binding proteins were eluted from S. pneumoniae as described above.
The proteins binding to the resins were eluted by the addition of three resin volumes of 20 mM Tris HCl, pH 8.0, and 1 M NaCl, and the elutes were collected in 2-ml fractions.
After extensive washing to remove non-specific binding, repeat-containing DNA fragments were eluted employing a magnetic particle concentrator.
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