Batroxobin is a thrombin-like proteolytic enzyme isolated from the venom of Bothrops atrox Maranhoa. It splits the 16 Arg-17 Gly bond in the Aα-chain of fibrinogen and causes the release of fibrinopeptide A and the formation of fibrin I monomer or Des-AA-monomer which spontaneously aggregates into a clot of fibrin I. Batroxobin also induces the release of tPA from endothelium.

Due to its specific action on fibrinogen and its ability to clot platelet-rich plasma without affecting the integrity and functions of the platelets, and thanks to its insensitivity to thrombin inhibitors, batroxobin has found several applications as a tool in blood coagulation research and diagnosis. Batroxobin can be used to determine fibrinogen in plasma, to measure the batroxobin clotting time (Reptilase time) as a heparin-insensitive parallel to the thrombin time, to investigate dysfibrinogenemia, and to test the contractile system of platelets.

Protac, a single chain glycoprotein, is a fast acting Protein C activator isolated from the venom of the copperhead snake Agkistrodon contortrix. It rapidly converts Protein C into Activated Protein C which may be determined either by measuring its prolonging effect on the activated partial thromboplastin time (APTT) or by measuring its enzyme activity by means of a specific chromogenic substrate.

Protac is used for the determination of Protein C and Protein S levels in plasma.

Packsize contains - 5 x 3 U vials

Protac, a single chain glycoprotein, is a fast acting Protein C activator isolated from the venom of the copperhead snake Agkistrodon contortrix. It rapidly converts Protein C into Activated Protein C which may be determined either by measuring its prolonging effect on the activated partial thromboplastin time (APTT) or by measuring its enzyme activity by means of a specific chromogenic substrate.

Protac is used for the determination of Protein C and Protein S levels in plasma.

For the determination of Prothrombin and Hirudin. Specifically activates prothrombin via meizothrombin.

Ecarin is a metalloprotease isolated from the venom of the saw-scaled viper (Echis carinatus) that activates prothrombin. Ecarin does not affect other clotting factors. The action of ecarin on prothrombin is independent of calcium, phospholipids and factor V. Moreover, Ecarin, in contrast to factor Xa, activates the acarboxy form of prothrombin present in plasma of patients undergoing oral anticoagulant therapy with vitamin K antagonists.

Determination of prothrombin levels in patients undergoing anticoagulant therapy. Based on the interaction of hirudin with meizothrombin a simple ecarin clotting test for the monitoring of hirudin levels has been developed (Nowak and Bucha, 1993). Due to its action on acarboxy prothrombin, ecarin can be used for the determination of acarboxy prothrombin in the supernatent of barium sulfate treated patient plasma where normal carboxylated prothrombin has been removed by adsorption. Ecarin can be used for the detection of low prothrombin concentrations in plasma fractions for quality- and in-process control purposes. Ecarin, used in conjunction with the phospholipid- and calcium ion-dependent prothrombin activator Textarin from Pseudonaja textilis venom, forms a highly sensitive and specific test system for lupus anticoagulant (Triplett et al., 1993).

Packsize contains 3 x 50 EU vials

For activation of human platelets via GPVI-receptor. Useful in studies on platelet receptors.

For activation and determination of Factor V.

For the determination of Factor X and for screening of Lupus Anticoagulants.

For the determination of Factor X and for screening of Lupus Anticoagulants.