Creative Biolabs is a recognized service provider in differential scanning calorimetry (DSC). DSC is a powerful analytical tool for characterizing the stability of proteins and other biomolecules directly in its native form with the aid of suitable thermodynamic models.

Introduction

DSC technique is very convenient requiring only minimal assay development, NO labeling or immobilization, and permits screening of large numbers of samples at low concentrations minimizing the consumption of valuable samples. It does this by measuring the heat change associated with the molecule’s thermal denaturation when heated at a constant rate. The resulting data provide critical guidance for biopharmaceutical development from protein engineering through pre-formulation and process development to formulation of the final product, driving productivity in biopharmaceutical research. We have reference samples meeting your requirement which are well-defined heat capacity over the range of temperatures to be scanned.

Key services we can supply include:

• Monitoring protein affinity, specificity and activity.
• Observing protein fusion and crystallization.
• Characterization and selection of the most stable proteins or potential candidates in biotherapeutic development and formulation.
• Studying protein-ligand interactions.
• Rapid optimization of purification and manufacturing conditions.
• Quick stability assays for target proteins to be used for screening.

Other optional antibody analysis services:

• Antibody Characterization
• Antibody Affinity Measurement
• Hybridoma Sequencing Service
• De Novo Antibody Sequencing Services
• Precision Paratope Mapping Service
• Monoclonal Antibody Epitope Binning
• SPR Services
• Isothermal Titration Calorimetry (ITC) Services
• Dual-Polarization Interferometry (DPI) Services

Published Data

• Analysis of IgG Kinetic Stability by DSC

Fig. 2 DSC reveals that thermal transitions are concentration‐independent. (Michal Nemergut, 2017)

Immunoglobulin G (IgG) type monoclonal antibodies are the mainstream therapy for many diseases, and their stability has great research potential. Here, the researchers used a series of methods to evaluate the kinetic stability of this type of antibody over a wide temperature range. To this end, they used the model IgG to carry out differential scanning calorimetry (DSC) experiments to test the exudate formula and the extended temperature range, and then analyzed the antibodies through the three-step sequence model of IgG denaturation developed by them. In summary, their studies have shown that this analysis can effectively evaluate the kinetic stability of IgG and accelerate the formulation development of monoclonal antibodies.

FAQ

1. What is Differential Scanning Calorimetry (DSC) and how is it used in antibody analysis?

   DSC is a thermal analysis technique that measures how the heat capacity of a sample changes as it is heated or cooled. In antibody analysis, DSC is used to study the thermal stability of antibodies by observing the temperature at which they undergo structural changes, such as unfolding or aggregation. This information is crucial for understanding the stability and shelf life of antibody products.

2. Why is thermal stability important for antibodies?

   Thermal stability is a key quality attribute for antibodies, especially those used in therapeutic applications. Stable antibodies are less likely to denature or aggregate under stress conditions, which can affect efficacy and safety. By using DSC to assess the thermal stability, researchers can predict how antibodies will behave during storage, transport, and in vivo conditions.

3. Can DSC differentiate between different forms of antibodies?

   DSC can differentiate between different forms or variants of antibodies based on their thermal stability profiles. Since each form may have a slightly different structure, they will typically exhibit different melting temperatures and thermal behaviors. This makes DSC a valuable tool for confirming the identity and purity of specific antibody forms in a sample.

4. What are the limitations of using DSC for antibody analysis?

   While DSC provides valuable information about the thermal stability and structure of antibodies, it does have some limitations. It generally requires a relatively high concentration of the sample, which might not be feasible for all types of antibodies or those available in limited quantities. Additionally, DSC does not provide information on the specific nature of structural changes or the functional activity of antibodies post-analysis.

5. What sample preparation is required for DSC analysis of antibodies?

   For DSC analysis, antibodies must be prepared in a suitable buffer at a concentration that ensures adequate signal detection without causing aggregation. Typically, concentrations around 0.5 to 1.0 mg/mL are used. The sample should be free from particulate matter, which may require filtration or centrifugation. Additionally, it's important to ensure that the pH and ionic strength of the buffer are appropriate for maintaining the stability of the antibodies during the analysis.

6. How does DSC contribute to the formulation development of therapeutic antibodies?

   DSC is instrumental in formulation development for therapeutic antibodies by identifying optimal conditions that enhance their thermal stability. By analyzing how different buffer compositions, pH levels, and excipients affect the thermal behavior of antibodies, researchers can design formulations that improve their stability, prolong shelf life, and enhance their delivery and efficacy in clinical applications.

7. Can DSC detect antibody-antigen interactions?

   While DSC is primarily used to study the thermal stability of proteins, it can indirectly detect changes in stability due to antibody-antigen interactions. If the binding of an antigen affects the conformational stability of an antibody, this may be reflected in changes in the antibody's thermal unfolding profile observed by DSC. However, specific binding interactions and their kinetics are better studied using other techniques like surface plasmon resonance or ELISA.

8. What are the advantages of DSC compared to other stability-assessment methods for antibodies?

   DSC is a label-free technique that does not require any modifications to the antibody or the use of secondary probes, which can alter protein properties. It provides a direct measurement of thermal stability through intrinsic properties of the protein, and it can comprehensively analyze the entire thermal unfolding process in a single, rapid experiment. Additionally, DSC can be highly reproducible and requires minimal sample preparation.

Resources

Use the resources in our library to help you understand your options and make critical decisions for your study.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.