Recombinant Human Serpin F2/alpha 2-Antiplasmin Protein, CF

Serpin F2 is a member of the Serpin superfamily and the primary physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots (1, 2). In addition to plasmin, Serpin F2 is also an efficient inhibitor of trypsin and chymotrypsin (3). Liver and kidney are major sites of Serpin F2 production and other tissues such as muscle, intestine, central nervous system, and placenta also express its mRNA at a moderate level. The tissue expression pattern of Serpin F2 indicates that it is a key regulator of plasmin-mediated proteolysis in these tissues (4). Human Serpin F2 is synthesized as a 491 amino acid precursor with a 27 amino acid signal peptide. The secreted protein has a short propeptide (residues 28-39) and a mature chain (residues 40-491). The presence of the propeptide did not affect its ability to inhibit plasmin but reduced its cross-linking ability to fibrin (5).