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The authenticity of binding was confirmed using cold competitors, both specific (self or consensus) as well as non-specific oligonucleotides.
Again binding was confirmed using specific and non-specific competitors.
Successful binding was confirmed using Fourier transform infrared spectroscopy (FTIR).
Linearity of [H]PiB binding was confirmed using 1 nM [H]PiB and 20 500 µg/ml of the Alzheimer's disease brain homogenate with the highest level of [H]PiB binding.
In silico analysis suggested that CRE1 3 contain one or more conserved SOX9-binding sites, and this binding was confirmed using chromatin immunoprecipitation on cells derived from mouse embryonic pharyngeal arch.
The specificity of binding was confirmed using an α-flag antibody that recognizes the epitope present in the N-terminal of mRARα and α-myc antibody that recognizes the epitope in the N-terminal of mRXRα.
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Successful functionalization of the lens surfaces with NH2 groups was required for peptide binding and was confirmed using methyl orange.
Specificity of VEGF-D binding to VEGFR3-765 was confirmed using a soluble VEGFR3/Fc chimera, which was able to compete with VEGFR3-765 binding to VEGF-D – unlike a soluble VEGFR1/Fc chimera.
The specificity of AZD2995 binding to amyloid-β was confirmed using binding and competition assays.
The specificity of Gal-binding by C. jejuni was confirmed using cell adherence assays, where a significant decrease was observed for 11168-GS grown at 37°C and 11168-O grown at 42°C following pre-treatment of Caco-2 cells with the lectin ECA.
In a first stage, the formation of stable reactive binding products of slate cement pastes was confirmed, using Vicat needle test and Scanning Electron Microscopy and Energy Dispersive Spectroscopy analysis (SEM/EDAX).
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