Recombinant Human Active Coagulation Factor XIV/ProteinC, CF

Protein C (PROC) is a vitamin K-dependent serine protease synthesized in liver as a single-chain precursor (1). The N-terminus consists of a signal peptide (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 serine protease domain (aa 212-450). Present in plasma at 3 to 5 mg/L, PROC plays a key role in anticoagulation. Physiologically, the inactive forms of PROC are converted to the active form by thrombin, which releases the activation peptide. The active PROC cleaves factors 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, PROC deficiency is caused by a genetic mutation which affects PROC activity. A severe recessive form may result in massive thrombosis fatal to patient.