The protein molecules in biotherapeutics must be in an active form and remain stable. Stability screening of biopharmaceuticals at the initial stage of development will help ensure and optimize the best conditions for drug development and rapid optimization of production conditions. Differential scanning calorimetry (DSC) can be used to quickly determine the optimal solution conditions for the stability of protein formulations, help determine the best candidate formulations and accelerate the development process, and indicate the stability of the target protein used for screening analysis. DSC data is very important for predicting the stability of protein in solution. It can be used for further stability, shelf life and transportation studies of formulations with the best thermal stability, and a fully automated system can improve key areas of biopharmaceutical research and development.
Creative Proteomics is a biopharmaceutical research partner with professional and high-quality proteomics research resources. We use first-class experimental platforms and powerful proteomics analysis methods to provide you with high-quality DSC services. The structural information analysis and stability of protein drugs in biotherapeutics are an indispensable part of protein drug quality control. We can provide a fully automated system for you to obtain accurate and highly accurate DSC analysis data and provide key information on the stability of protein molecules in the development of potential candidate biotherapeutics.
We Can Provide but Not Limited to:
- Analysis of protein structure stability
- Protein molecular stability analysis
Technology Platform of Differential Scanning Calorimetry Service:
Creative Proteomics provides efficient and accurate detection and data analysis of protein stability by providing Differential Scanning Calorimetry (DSC) technology.
We provide the following analysis methods:
Differential scanning calorimetry
The stability data analysis of protein molecules is generated and analyzed by measuring the heat change data related to the thermal denaturation of protein molecules when heated at a constant rate. The specific workflow is as follows.
Advantages of Differential Scanning Calorimetry Service:
- Short time-consuming: The technology uses advanced experimental equipment and simple experimental methods, which greatly reduces the time for protein stability analysis.
- High sensitivity: The equipment used in the DSC service has high sensitivity, and a high-quality data report can be obtained with a small amount of samples to be tested.
- High quality: In this service, the types of proteins to be tested are diverse, and multiple samples can be tested at the same time.
- High accuracy: The experimental equipment in DSC technology has high accuracy, and adopts fully automatic experimental operation methods and data analysis procedures to greatly improve its accuracy.
- Rapid turnaround time: 5-7 days to provide detailed technical reports.
- Customized service: We can customize professional solutions for you according to your research plan needs. You can select or suggest the required items for analysis.
Creative Proteomics's professional researchers can provide customers with accurate and high-quality DSC analysis data and provide information about the stability of proteins in biotherapeutics during process development. Protein stability analysis and research can provide key information for the optimization of conditions for the development of biologics to accelerate the pace of biotherapeutic drug development. We will provide you with a comprehensive experimental operation plan and the final analysis report of protein stability results and other data analysis reports. We are committed to providing you with professional services on the stability of protein molecules in biotherapeutics to help you solve related technical problems.
References
- Spink CH. Differential scanning calorimetry. Methods Cell Biol. 2008.
- Cañadas O, Casals C. Differential Scanning Calorimetry of Protein-Lipid Interactions. Methods Mol Biol. 2019.
