Prionex® 10% Reference: 069-03 Prionex® is a 10% aqueous solution of a polypeptide fraction of highly purified dermal collagen of porcine origin which has excellent protein stabilizing properties. Prionex® is prepared by partial hydrolysis and is terminally sterilized. It is free from cartilage, bone and plasma components and is therefore a pure form of partially hydrolyzed gelatine type A. The average molecular weight is approx. 20’000 Da, estimated by gel permeation chromatography. Prionex® is freely soluble in water, diluted electrolyte solutions, glycerol and DMSO as well as in diluted ethanol and ammonium sulphate solutions below 20% saturation. Storage: 15 - 25°C, protected from light, Optimizes stability of biological activity, Improves conditions for lyophilisation and heat treatment, Avoids denaturation by chaotropic agents or solvents, Extends shelf life for enzymes and proteins, High consistency stabilizer, Non-toxic and non-antigenic, Free from nucleic acids, polysaccharides and lipids, Free from any additives
Rabbit brain cephalin, freeze dried Reference: 801682 Rabbit brain cephalin consists of phospholipids isolated from rabbit brain. It can be used as a phospholipid source in phospholipid dependent coagulation assays. The main components are: Phosphatidylserine, Phosphatidylethanolamine, Phosphatidylethanolcholine
Defibrase® Reference: 101-04 101-06 Defibrase® is the trademark registered by Pentapharm for its Active Pharmaceutical Ingredient (API) Batroxobin, a serine protease. Batroxobin is a thrombin-like enzyme purified from the snake venom of Bothrops moojeni. Batroxobin is a pure single-chain glycopeptide with a molecular weight of approx. 32’600 Dalton. In contrast to thrombin, which converts fibrinogen into fibrin by splitting off fibrinopeptides A and B, batroxobin only splits off fibrinopeptide A. The enzyme has a defibrinogenating effect and is used clinically for the treatment of thrombotic diseases.
Protac® Reference: 113-01 113-05 Protac®, a single chain glycoprotein, is a fast-acting protein C activator isolated from the venom of the copperhead snake Agkistrodon contortrix and closely related snake species. This serine proteinase rapidly converts protein C of man and other vertebrates 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.
Ecarin Reference: 116-01 Ecarin is a 55’000 to 60’000 Da 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.
Convulxin Reference: 119-02 Convulxin, a 84'000 Da heterodimeric C-type lectin isolated from Crotalus durissus terrificus venom, activates mammalian platelets via binding and clustering of GPVI-receptors under physiological conditions. Occupation and clustering of GPVI activates Src family kinases, phosphorylating Fc receptor ɣ-chain and activating p72SYK that is critical for downstream activation of platelets.
RVV-Factor X Activator Reference: 121-06 121-07 Specific 120’000 Da factor X activator from Russell’s viper venom. RVV-X is a dimer of two peptide chains with a molecular weight of 60’000 g/mol each. Activation of factor X by RVV-X strictly depends on the presence of calcium ions.