Related Experiment Video
Updated: Feb 7, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Long-Term Stability and Reversible Thermal Unfolding of Antibody Structure at Low pH: Case Study
Harumi Fukada1, Kouhei Tsumoto2, Tsutomu Arakawa3
1Graduate School of Science, Osaka Prefecture University, Naka-ku, Sakai, Osaka 599-8531, Japan.
Abstract:
We have here observed that the differential scanning calorimetry profiles and melting temperatures of a humanized antibody were unchanged over a 10-year span when stored at 4°C and at different pH values, even at pH 2.7. This is somewhat surprising, as this particular antibody undergoes conformational changes below pH 4.0. Differential scanning calorimetry analysis showed that melting of the antibody at pH 2.7 was highly reversible, suggesting a possibility that the observed reversibility is at least in part responsible for a 10-year stability at low pH. Conversely, it showed thermal unfolding followed by aggregation at higher pH.
More Related Videos
Related Concept Videos
Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Stability of structures
Antibody Structure and Classes
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
The Unfolded Protein Response
RNA Stability
Nuclear Stability
To hold positively charged protons together...

