Proteases (Serine)
The large family of serine proteases (almost one-third of all proteases; EC 3.4.21.-) is characterized by its general mechanism of action to cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. The members of this family can be divided roughly into four sub-groups based on their structure, being chymotrypsin-like (trypsin-like), subtilisin-like, carboxypeptidase Y-like, and Clp-like[1].
[1] L. Hedstrom. Serine Protease Mechanism and Specificity. Chem. Rev. 2002, 102, 4501-4524.
| Axon ID | Name | Description | From price | |
|---|---|---|---|---|
| 3590 | ACT001 | PAI-1 inhibitor | €210.00 | |
| 3568 | Col003 | Potent, competitive collagen-Hsp47 interaction inhibitor | €110.00 | |
| 3294 | HSP47 inhibitor III | Inhibitor of the collagen-specific chaperone HSP47 | €120.00 | |
| 3710 | PAZ-417 | Potent, orally active and CNS-penetrant PAI-1 inhibitor | €130.00 | |
| 2838 | SK-216 | Specific inhibitor of PAI-1 | €105.00 | |
| 1769 | T 1776Na | Inhibitor of plasminogen activator inhibitor-1 | €80.00 | |
| 1383 | Tiplaxtinin | Plasminogen activator inhibitor-1 (PAI-1) inhibitor | €70.00 | |
| 2344 | TM 5275 | Selective and orally active inhibitor of PAI-1 | €105.00 | |
| 2734 | TM 5441 | Orally active inhibitor of PAI-1 | €105.00 | |