Related Experiment Video
Updated: Jul 4, 2026
Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
Published on: July 21, 2021
Design of a fluorescence polarization assay platform for the study of human Hsp70
Yanlong Kang1, Tony Taldone, Cristina C Clement
1Program in Molecular Pharmacology and Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Abstract:
The 70kDa heat shock proteins (Hsp70) are molecular chaperones that assist in folding of newly synthesized polypeptides, refolding or denaturation of misfolded proteins, and translocation of proteins across biological membranes. In addition, Hsp70 play regulatory roles in signal transduction, cell cycle, and apoptosis. Here, we present a novel assay platform based on fluorescence polarization that is suitable for investigating the yet elusive molecular mechanics of human Hsp70 allosteric regulation.
