SERPINF2 is a glycoprotein composed of a single polypeptide chain with approximately 11.7% carbohydrate content . It is a potent and rapidly acting inhibitor of plasmin, the enzyme responsible for breaking down fibrin in blood clots . By inhibiting plasmin, SERPINF2 helps maintain the stability of blood clots, which is essential for proper wound healing and prevention of excessive bleeding.
The gene encoding SERPINF2 is located on chromosome 17 in humans and has several aliases, including A2AP, API, and PLI . Multiple transcript variants encoding different isoforms have been identified for this gene . Mutations in the SERPINF2 gene can lead to alpha-2-plasmin inhibitor deficiency, a condition characterized by severe hemorrhagic diathesis .
SERPINF2 is involved in various biological pathways, including the response to elevated platelet cytosolic Ca2+ and diseases of hemostasis . It also interacts with other proteins, such as matriptase-3/TMPRSS7 and chymotrypsin, further highlighting its importance in regulating proteolytic activities in the body .
Recombinant mouse SERPINF2 is produced using recombinant DNA technology, which involves inserting the gene encoding SERPINF2 into a suitable expression system, such as bacteria or mammalian cells. This allows for the production of large quantities of the protein for research and therapeutic purposes. Recombinant SERPINF2 is used in various studies to understand its role in fibrinolysis and to develop potential treatments for bleeding disorders.
The proper function of SERPINF2 is vital for maintaining hemostasis, the process that stops bleeding at the site of an injury while keeping blood in a fluid state within the vascular system. Deficiencies or dysfunctions in SERPINF2 can lead to bleeding disorders, making it a critical target for therapeutic interventions .