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Finally the tightly binding proteins are eluted with excess free drug or under highly denaturing conditions.
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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.
AAV-ITR binding proteins were eluted out, dialyzed overnight following the instruction of the kit, and subjected to western blot analysis.
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.
The DENV-2 binding proteins were eluted with 0.1 M glycine-HCl pH 2.7 or buffer E containing 1 M NaCl.
The drug-binding proteins are eluted from the affinity beads with a high salt solution or a detergent containing solution following brief centrifugation.
Binding protein was eluted by the same buffer, the eluted protein was pooled and loaded on an anion-exchange Mono Q column which was equilibrated with 20 mM Tris HCl buffer (pH 8.2).
Choline-binding proteins were eluted from S. pneumoniae as described above.
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