Acridinium-Based Chemiluminescent Receptor-Ligand Binding Assay for Protein/Peptide Hormones

Abstract

Chemiluminescent acridinium esters (AE) have been extensively used for oligonucleotide probing and peptide-binding assays in molecular research due to labeling efficiency, lack of radioactivity, and ease of application. In addition to being a powerful and reliable alternative to radiolabeling, AE can be directly bound to the target molecule, with high specificity. Here, we describe an AE-based protein/peptide labeling method and the use of the labeled protein/peptide in a ligand-binding assay.

Keywords: Aequorin; Binding assay; Ca2+ mobilization assay; Chemiluminescence; HPLC purification; Peptide labeling; Peptide purification; Receptor-ligand interaction.