Analysis of the thermal stability of peptide-MHC complexes by Differential Scanning Fluorimetry(DSF) (CAT#: STEM-MB-0766-WXH)

Introduction

The major histocompatibility complex (MHC) is a large locus on vertebrate DNA containing a set of closely linked polymorphic genes that code for cell surface proteins essential for the adaptive immune system. These cell surface proteins are called MHC molecules.
Quantifying the strength of the interactions between peptides and major histocompatibility complex (MHC) proteins is important in the identification of T cell epitopes and evaluating the consequences of naturally occurring or engineered peptide modifications.

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Principle Applications Procedure Materials Notes Related Products

Principle

Differential Scanning Fluorimetry measures protein thermal unfolding by monitoring changes in fluorescence emission of a sample upon heating. This allows the determination of protein thermostability and complex formation even with weakly binding ligands by thermal shift assay. Differential Scanning Fluorimetry is therefore ideally suited for screening of optimum buffer conditions like pH, buffer composition and ionic strength. The technique is applicable to any biological sample, from soluble proteins to integral membrane proteins.

Applications

To identify low-molecular-weight ligands that bind and stabilize purified proteins.
To measure the denaturation and unfolding of proteins.

Procedure

1. Preparation of compound solutions
2. Preparation of buffer/additive screen plates
3. Preparation of compound storage plates
4. Equipment preparation
5. Sample preparation
20. Performing the scan

Materials

Real-time PCR instrument

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