Lepirudin is a recombinant hirudin derived from yeast cells. It is almost identical to hirudin extracted from Hirudo medicinalis. Lepirudin is a highly specific direct inhibitor of thrombin.
CAT No: 10-101-90
CAS No:138068-37-8 (net)
Synonyms/Alias:(Leu1,Thr2)-Hirudin (desulfated); Lepirudin; Refludan; Refludin; Hbw 023; Hbw-023; Hbw023
Lepirudin, a recombinant hirudin derived from yeast cells, is a highly specific and potent direct thrombin inhibitor. Unlike traditional anticoagulants, Lepirudin does not require antithrombin as a cofactor, allowing it to bind directly to thrombin and inhibit its activity with remarkable specificity. Its structure, closely resembling natural hirudin, enables effective blockade of both free and clot-bound thrombin, making it a valuable tool in settings where precise modulation of coagulation is required. The recombinant nature of Lepirudin ensures batch-to-batch consistency, reducing the risk of immunogenic reactions associated with animal-derived products, and its stability in various experimental conditions further enhances its utility in scientific investigations.
Coagulation Research: In coagulation research, Lepirudin is extensively utilized for its ability to provide a clear and direct assessment of thrombin's role in the blood clotting cascade. By selectively inhibiting thrombin, researchers can dissect the contributions of downstream coagulation factors and study the dynamics of fibrin formation and platelet activation. Experimental protocols often employ this direct thrombin inhibitor to create controlled models of anticoagulation, facilitating the evaluation of novel anticoagulant candidates or the elucidation of pathological mechanisms underlying hypercoagulable states. Its predictable pharmacodynamic profile allows for reproducible results in both in vitro and ex vivo studies, thereby supporting high-quality research outputs.
Platelet Function Studies: For investigations into platelet biology, Lepirudin serves as a valuable tool to isolate the effects of thrombin from other platelet agonists. By neutralizing thrombin activity, scientists can differentiate between thrombin-dependent and thrombin-independent pathways in platelet aggregation and secretion assays. This separation is crucial for understanding the complex interplay between coagulation and platelet activation, particularly in the context of thrombosis research. The use of Lepirudin in these assays ensures that observed platelet responses are not confounded by residual thrombin, yielding more accurate insights into platelet physiology and the mechanisms of antiplatelet agents.
Proteomics and Thrombin Substrate Identification: In proteomics, the application of Lepirudin is instrumental for characterizing thrombin substrates and mapping cleavage sites within complex biological samples. By selectively blocking thrombin activity, researchers can prevent post-sampling proteolysis, preserving the native state of proteins and enabling precise identification of thrombin-specific cleavage events. This approach aids in the discovery of novel thrombin substrates and the clarification of its broader biological roles, which is essential for advancing therapeutic strategies targeting thrombin-mediated processes. The use of recombinant hirudin in proteomic workflows enhances data reliability and supports the development of new analytical methodologies.
Biomaterial and Device Testing: The evaluation of blood-contacting biomaterials and medical devices often necessitates the use of anticoagulants to prevent clot formation during testing. Lepirudin is frequently chosen for these applications due to its direct and effective inhibition of thrombin, which minimizes the risk of device-induced thrombosis in experimental setups. Its compatibility with a wide range of materials and assay systems allows for accurate assessment of hemocompatibility, surface-induced coagulation, and device performance under physiologically relevant conditions. Employing Lepirudin in these studies helps to ensure that the observed effects are attributable to the material or device itself, rather than confounding influences from the coagulation cascade.
Cellular Signaling Pathway Analysis: The role of thrombin extends beyond coagulation, influencing various cellular signaling pathways involved in inflammation, tissue remodeling, and angiogenesis. Lepirudin is utilized in cell-based assays to dissect the specific contributions of thrombin to these processes. By inhibiting thrombin, researchers can evaluate changes in gene expression, cytokine release, and cellular behavior in response to different stimuli, thereby unraveling the multifaceted roles of thrombin in cellular physiology. This application is particularly valuable in studies aiming to identify new therapeutic targets or to understand the molecular mechanisms underlying thrombin-mediated cellular responses.
Biochemical Assays and Method Validation: In the realm of biochemical assay development, Lepirudin is employed to validate the specificity and sensitivity of thrombin detection methods. Its high affinity for thrombin provides a reliable means of establishing assay baselines and negative controls, ensuring that detected signals are truly thrombin-dependent. Method validation studies often incorporate Lepirudin to confirm assay performance across various sample types, contributing to the development of robust analytical platforms for research and diagnostic applications. The versatility of this recombinant inhibitor supports its widespread adoption in laboratories focused on thrombosis, hemostasis, and protease biology.
Lepirudin is indicated for anticoagulation in patients with heparin-induced thrombocytopenia (HIT). We describe 2 cases of HIT and thrombosis in children with heart disease, including one that required extracorporeal membrane oxygenation. Lepirudin, dosed in the recommended adult weight--based fashion, was an effective antithrombotic agent in pediatric patients with HIT.
Deitcher, S. R., Topoulos, A. P., Bartholomew, J. R., & Kichuk-Chrisant, M. R. (2002). Lepirudin anticoagulation for heparin-induced thrombocytopenia. The Journal of pediatrics, 140(2), 264-266.
Lepirudin is one of few anticoagulants that can be safely used in patients with HIT. Because it is eliminated through the kidneys, great care must be taken when administering lepirudin to patients with renal failure; in fact, its use is currently not recommended in patients requiring hemodialysis. Lepirudin effectively prevented acute thrombosis in both of our patients with documented HIT, with no bleeding complications. We describe how we selected the initial doses and report results of aPTT monitoring.
Dager, W. E., & White, R. H. (2001). Use of lepirudin in patients with heparin-induced thrombocytopenia and renal failure requiring hemodialysis. Annals of Pharmacotherapy, 35(7-8), 885-890.
Lepirudin (Refludan), Berlex Laboratories, USA and Canada; Pharmion, all other countries), a recombinant derivative of the naturally occurring leech anticoagulant hirudin, was the first direct thrombin inhibitor to be approved by the European Agency for the Evaluation of Medicinal Products and the US Food and Drug Administration for the treatment of heparin-induced thrombocytopenia. Since its introduction into Europe and the USA, it has been studied in over 7000 patients requiring anticoagulation in conditions including acute coronary syndromes, percutaneous coronary intervention, cardiopulmonary bypass and heparin-induced thrombocytopenia. Three European clinical trials, designated Heparin-Associated Thrombocytopenia (HAT)-1, -2 and -3, demonstrated the efficacy and safety of lepirudin in the prevention and treatment of thrombosis in patients with antibody-confirmed heparin-induced thrombocytopenia.
Greinacher, A. (2004). Lepirudin: a bivalent direct thrombin inhibitor for anticoagulation therapy. Expert review of cardiovascular therapy, 2(3), 339-357.
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