F7 Human

Recombinant factor VIIa is a vitamin K-dependent glycoprotein consisting of 406 amino acid residues. It is produced using recombinant DNA technology, where the gene encoding human factor VII is cloned and expressed in mammalian cells, typically baby hamster kidney (BHK) cells . The protein is then purified and activated to its functional form, which is a two-chain structure .

The primary function of recombinant factor VIIa is to promote hemostasis by activating the extrinsic pathway of the coagulation cascade. It achieves this by binding to tissue factor (TF) exposed at the site of vascular injury. This complex then activates factor X to factor Xa, which, in turn, converts prothrombin to thrombin. Thrombin is a key enzyme that converts fibrinogen to fibrin, forming a stable blood clot .

Recombinant factor VIIa is primarily used to treat bleeding episodes in patients with hemophilia A or B who have developed inhibitors against factor VIII or IX . It is also used in patients with acquired hemophilia, congenital factor VII deficiency, and Glanzmann’s thrombasthenia with refractoriness to platelet transfusions . Additionally, it is employed in surgical settings to manage bleeding in patients with these conditions .

Recombinant factor VIIa is administered via intravenous injection. The dosage and frequency of administration depend on the severity of the bleeding episode and the patient’s clinical condition. The most common side effects include venous thromboembolic events, rash, pruritus (itching), urticaria (hives), fever, and reduced effectiveness of treatment .

The development of recombinant factor VIIa began in the 1980s, with the first recombinant product becoming available in 1988 . The currently marketed product, NovoSeven, was approved by the United States Food and Drug Administration (FDA) in 1999 for use in treating bleeding episodes in patients with congenital hemophilia A or B with inhibitors . Since then, several biosimilar products have been developed and approved for clinical use .