Recombinant Human Coagulation Factor XIV/Protein C, CF

Protein C, also known as Coagulation Factor XIV, is a vitamin K-dependent serine protease synthesized in the liver as a single-chain precursor (1). The N‑terminus consists of a signal peptide (amino acid (aa) 1-32) and a propeptide (aa 33-42). The mature chain (aa 43‑461) is converted to two disulfide-linked chains (light: aa 43‑199 and heavy: 200-461) and both forms are inactive. The light chain consists of Gla (gamma-carboxy-glutamate) domain and two EGF-like domains. The heavy chain consists of an activation peptide (aa 200‑211) and a serine protease domain (aa 212-450). Present in plasma at 3 to 5 mg/L, protein C plays a key role in anticoagulation. Physiologically, the inactive forms of protein C are converted to the active form by thrombin, which releases the activation peptide. The active protein C cleaves factor VIIIa and Va to inactivate them. This anticoagulation activity can be enhanced by a presence of a cofactor such as protein S. In hereditary thrombophilia, protein C deficiency is caused by a genetic mutation which affect protein C activity. A severe recessive form may result in a massive thrombosis, which is fatal to the patient. The recombinant human Protein C consists of both the mature chain and the two disulfide-linked chains, which can be activated by treatment with thermolysin.