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Materials, such as cells and plasmids, and methods for protein purification, crystallization and the PS binding assay can be found in the Supplementary Materials.

In summary, if the mechanism of action of therapeutic mAbs expected to be binding activity to a specific ligand, the binding assay can be used as lot release assay along with the cell-based assay during clinical development phases.

Given the sensitivity and unambiguous binding data, artifacts that plague nearly every other binding assay can be avoided.

Therefore, direct in vivo approaches like imaging techniques using microscopy-based binding assay can be exploited for high temporal resolution measurements of components kinetics and may be a more favourable option [ 105].

We believe that some competitive binding assays can be carried out using a cocktail of receptors at the same time if interference among different assay systems can be avoided by choosing ideal conditions.

In conclusion, both the soluble receptor-based and cell-based binding assays can be used to identify IgG1 variants with increased affinity to FcγRIIIa and unaltered affinity to FcγRI and FcRn.

A general scheme demonstrating how competitive binding assays can be used to identify substrate phosphorylation site inhibitors is shown in Scheme 3.

Even though the ligand-binding assay can be performed readily with desirable precision and accuracy, the mechanism of action could involve downstream events post ligand-binding.

To identify TH-disrupting compounds in the environment, the TTR-binding assay can be used in effect-directed analysis (EDA).

Binding assays can be used to either directly detect binding of a ligand to the target or indirectly detect binding through competitive displacement of a probe.

Therefore, our study indicates that this direct protein ligand binding competitor assay can be used as an effective alternative method in the early screening of PPARγ ligands.