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(A) Solid-phase binding assay for FtsZ and Ga5DH.
A competitive binding assay for biotin, biocytin, and desthiobiotin utilizing a genetically engineered enzyme ligand conjugate is described herein.
One of the compounds with a promising kinetic selectivity profile was also examined in a [35S]-GTPγS binding assay for functional activity.
Among them, p-carboranylcyclohexanol derivatives 8a and 8b exhibited high ERβ selectivity in competitive binding assay: for example, 8a showed 56-fold selectivity for ERβ over ERα.
Therefore, we have developed a biomimetic surface imprinting strategy for QCM studies of D1R-ligand binding and presented a new method to ligand binding assay for D1R.
The ELISA binding assay for 89Zr-bevacizumab gave a binding of 75%, which is optimal for this assay, and did not alter upon coupling of 1 of 2 eq of dye.
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Final compounds were evaluated in radioligand binding assays for their ability to interact with 5-HT6 receptors.
To develop mAb-specific binding assays for each antitoxin, we mapped the epitopes of the six mAbs.
(C) In vitro binding assays for analysis of the binding of recombinant KDM5B variants to the unmodified histone H3K4 N-terminal tail.
In vitro binding assays for VAChT were conducted with human VAChT stably expressed in PC12A123.7 cells at about 50 pmol/mg of crude extract.
Some synthesized compounds, tested in binding assays for the human cloned α1A-, α1B-, and α1D-AR subtypes, displayed affinities in the nanomolar range.
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