Biomolecular interactions are crucial for biological processes like transcription, translation, and cell signaling. These interactions have been targeted for drug development. Traditional assay formats used to measure these interactions have limitations, as they can only measure a limited range of dissociation constants (KD), often in the nanomolar range.

AlphaLISA™ can study a wide range of biomolecular interactions and detect a broad range of affinities with KD ranging from picomolar to low millimolar.

In this application note, we demonstrate how AlphaLISA can be used to measure three very different types of biomolecular interactions with three very different binding affinities:

• TDP-43 protein binding to TAR-32 DNA oligo (KD < 1 nM),
• MDM2 protein binding to p53 protein (KD= 0.3 μM),
• and two different lectins binding a glycosylated antibody (KD > 10 μM).

For research use only. Not for use in diagnostic procedures.