Aprotinin Reference: 073-70 800277 Aprotinin is a polypeptide extracted from bovine lung and composed of 58 amino acids with a molecular weight of 6’512 Daltons. Aprotinin is a polyvalent reversible inhibitor of serine proteinases including plasmin and kallikrein. The active loop contains the reactive lysine residue in position 15, the tertiary structure shows a pear-shaped unit which fits exactly into the binding site of serine proteinases. Aprotinin slows down fibrinolysis, the process that leads to the breakdown of blood clots. In addition to its anti-fibrinolytic activity, aprotinin is also thought to preserve platelet function and have anti-inflammatory effects, both of which may be mediated by inhibition of protease-activated receptors expressed on platelets, vascular endothelium, and neutrophils.
Pefabloc® SC Reference: 399-01 C8H10FNO2S · HCl Pefabloc® SC is an irreversible proteinase inhibitor with broad specificity for serine proteinases.
Pefabloc® FG Reference: 099-01 H-Gly-Pro-Arg-Pro-OH · AcOH Pefabloc® FG binds with a high affinity to fibrinogen, inhibits fibrin polymerization, modifies the mechanical properties of fibrin clots and can dissociate non-stabilized fibrin gels.
Pefabloc® TH (α-NAPAP) Reference: 381-01 C27H31O4N5S · AcOH Nα-(2-Naphthylsulfonylglycyl)-4-amidino-(D,L)-phenylalanine piperidide · AcOH Pefabloc® TH (NAPAP) is one of the most potent and selective competitive inhibitors of thrombin.
r-hirudin EC Reference: 126-10 Hirudin is the most potent and specific thrombin inhibitor known. It forms a stable equimolar complex with thrombin. The complete structure of hirudin has been elucidated [Dodt et al., 1984] and a gene coding for hirudin was subsequently synthesized and expressed in yeast [Meyhack et al., 1987] and other micro-organisms. The amino acid sequence of recombinant hirudin (r-Hirudin, [Leu1, Thr2]-63-desulfatohirudin) corresponds to natural hirudin except for the substitution of leucine for isoleucine at the Nterminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63.
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.