Analysis Interactions of PD-1/PD-L1 by Microscale Thermophoresis (MST) (CAT#: STEM-MB-2460-LGZ)

Introduction

The characterization of protein interactions has become key to many areas of life sciences, especially drug discovery. Microscale Thermophoresis (MST) is a new method for the quantitative analysis of protein-protein interactions (PPIs) with low sample consumption. Furthermore, one of the main advantages of this technique is that no tedious purification steps are required to obtain the protein of interest. MST can be determined the binding affinity of the PD-1/PD-L1 couple, which is involved in tumor escape processes, without purification of the target protein from cell lysates.

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Principle Applications Procedure Materials Notes Related Products

Principle

One of the interacting molecules (mostly proteins) is labeled with fluorescent dye or combined with GFP label. The labeled protein and ligand molecules are placed in the capillary according to a specific concentration gradient. Infrared laser heating generates a microscopic temperature gradient field to undergo thermophoresis, with which the hydration layer, molecular size, electric charge and other molecular properties will change. Then the fluorescence distribution in the reaction system changes. In addition to accurately detecting interactions between biomolecules, MST can also obtain other parameters related to interactions between biomolecules by calculating dissociation constants (Ks), and achieve accurate qualitative analysis.

Applications

For characterizing thermodynamic parameters of biomolecular interactions.

Procedure

1. Sample processing.
2. MST detection.
3. Data analysis.

Materials

• Sample Type: protein 10uM/ 100ul or 50 micrograms, small molecules 100uM/200ul, protein peptides need to be sent at low temperature

Notes

In order to ensure the reliability of the test, some samples should be provided as much as possible.

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