Characterizing binding interaction between PD-1-PD-L1 directly from cell lysates using MST

The involvement of the immune system in tumor control is becoming well understood. The tumor environment is in a state of equilibrium between the elimination of cancer cells by the immune system and their proliferation. The immuno-evasion mechanisms that allow tumor cells to remain in equilibrium with the host depends on the overexpression of immunoregulatory molecules such as PD-L1 and its interaction with PD-1 expressed on tumor-infiltrating T lymphocytes. Blocking this interaction is being considered as a more targeted therapeutic approach that blocks the interaction of PD-1 with its ligands, leading to various clinical trial using monoclonal antibodies anti-PD-1 or anti-PD-L1 in several types of cancers. In order to develop such therapies, it is imperative to characterize the interaction between PD-1 and PD-L1. In this webinar we will show how we employed MicroScale Thermophoresis (MST) for the quantitative analysis of the binding affinity between these two molecules. Particularly we describe a method that utilizes low sample consumption and no tedious purification step of the protein of interest.

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Receptor kinase THESEUS1 is a rapid alkalinization factor 34 receptor in Arabidopsis
Receptor kinase THESEUS1 is a rapid alkalinization factor 34 receptor in Arabidopsis

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Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site
Substrate-bound outward-open structure of a Na+-coupled sialic acid symporter reveals a new Na+ site

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