Analysis Interactions of Protein-Lipid by Microscale Thermophoresis (MST) (CAT#: STEM-MB-2463-LGZ)

Introduction

The ability to determine the binding affinity of lipids to proteins is an important component in understanding protein-lipid interactions in membrane trafficking, signal transduction, and cytoskeletal remodeling. Classic tools to measure such interactions include surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC). While these methods are powerful tools, they also have setbacks. ITC requires large quantities of purified proteins and lipids, which can be expensive and difficult to produce. Furthermore, both ITC and SPR are time-consuming, which can significantly increase the cost of performing these experiments. One way to get around these limitations is to use the relatively new technique of microscale thermophoresis (MST). MST is a fast and cost-effective method that requires only a small amount of sample to obtain a saturation curve for a given binding event.