Analysis of antibody CH2 domain by Differential Scanning Fluorimetry(DSF) (CAT#: STEM-MB-0815-WXH)

Introduction

CH2 domain is a region of the effector region of IgG, termed Fc, and includes a N-glycosylation site. Notably, the CH2 domain is a promising scaffold candidate for developing novel therapeutics because it can potentially target epitopes not accessible by full-size antibodies. Among the immunoglobulin domains, the CH2 domain has the lowest thermal stability, which also depends on amino acid sequence and buffer conditions.

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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
69. Performing the scan

Materials

Real-time PCR instrument

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