Human tissue plasminogen activator, purified, glycosylated, 355 residues purified from CHO cells. Retavase is taken into consideration a "third-era" thrombolytic agent, genetically engineered to hold and delete positive portions of human tPA. Retavase is a deletion mutein of human tPA shaped by means of deleting numerous amino acids present in endogenous human tPA. Retavase incorporates 355 of the 527 amino acids of native human tPA (amino acids 1-3 and 176-527), and retains the pastime-related kringle-2 and serine protease domain names of human tPA. three domain names are deleted from retavase - kringle-1, finger, and epidermal growth issue (EGF).
Reteplase cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. This helps eliminate blood clots or arterial blockages that cause myocardial infarction.
For lysis of acute pulmonary emboli, intracoronary emboli and management of myocardial infarction
Reteplase binds to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain. The protease domain then cleaves the Arg/Val bond in plasminogen to form plasmin. Plasmin in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action.