Reproducibility is a key tenet of scientific research, but many pharma groups have projects that collaborate across different sites or that rely on materials prepared by other specialist companies. With this in mind, group directors recognize the importance of having a clear-cut, industry-wide standard for any protocol that will require cross-site or cross-user validation. That’s where DIN SPECs come in.
A DIN SPEC is a protocol or specification (SPEC) that is reviewed and approved by the German Institute of Standardisation (DIN), an independent standardization body. Though a DIN SPEC is approved by a German institute, there are processes and standards that have gone through this approval and have become international standards — one notable example is A4 size paper.
NanoTemper Technologies and 2bind announced the approval of a DIN SPEC, which outlines how to best perform thermal unfolding experiments with a variety of approaches, specifically extrinsic differential scanning fluorimetry (DSF), differential scanning calorimetry (DSC), and nanoDSF technologies. This enables any researcher in the pharmaceutical space to carry out experiments using a protocol that produces reliable data about their protein’s thermal stability characteristics.
To make certain there is objectivity in creating a DIN SPEC, it must be written and endorsed by a third-party user. 2bind, who drove the process to write this SPEC, brought practical knowledge from their experience using these technologies, such as nanoDSF, which is available in the Prometheus instrument. Working with a third party ensures that other users who reference the SPEC for their own workflows have an accessible, credible source to use for their own internal SOPs.
Researchers in the pharmaceutical space require methodologies that will give reliable data, regardless of who performs them. This DIN SPEC is a first step towards establishing industry-wide SOPs when it comes to protein characterization experiments. To learn more about DSC, DSF, and nanoDSF, read The definitive guide to understanding protein stability.