| Filed | Form | Description | |
|---|---|---|---|
| 2/23/26 | DEFA14A | DEFA14A | → |
| 2/18/26 | DEFA14A | DEFA14A | → |
| 2/13/26 | DEFA14A | DEFA14A | → |
| 2/3/26 | DEFA14A | DEFA14A | → |
| 1/30/26 | DEFM14A | DEFM14A | → |
| 1/12/26 | DEFA14A | DEFA14A | → |
| ↓ | |||
| Filed | Form | Description | |
|---|---|---|---|
| 2/27/26 | 4 | 4 | → |
| 2/27/26 | 4 | 4 | → |
| 2/27/26 | 4 | 4 | → |
| 2/27/26 | 4 | 4 | → |
| 2/27/26 | 4 | 4 | → |
| 2/27/26 | 4 | 4 | → |
| ↓ | |||
In biochemistry, avidity refers to the accumulated strength of multiple affinities of individual non-covalent binding interactions, such as between a protein receptor and its ligand, and is commonly referred to as functional affinity. Avidity differs from affinity, which describes the strength of a single interaction.