Thrombin Human Recombinant
Thrombin Human Recombinant, HEK
Thrombomodulin Human Recombinant
Recombinant human THBD, expressed in Sf9 insect cells using a baculovirus expression system, is a single, glycosylated polypeptide chain. This protein consists of 500 amino acids (residues 22-515) with an approximate molecular weight of 52.6 kDa. For purification purposes, a 6-amino acid Histidine tag is fused to the C-terminus. The protein is purified using proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Sterile Filtered, lyophilized powder with a beige color.
Thrombin, also known as coagulation factor IIa, is a serine protease that plays a crucial role in the blood coagulation process. It is derived from its inactive precursor, prothrombin, through enzymatic cleavage by the prothrombinase complex . Thrombin is classified as a serine protease due to its mechanism of action involving a serine residue at its active site .
Key Biological Properties: Thrombin is a Na±activated, allosteric enzyme that exists in multiple forms, including E*, E, and E:Na+, which interconvert based on ligand binding . It is involved in various physiological processes, including blood coagulation, cell-mediated immunity, and cell death .
Expression Patterns and Tissue Distribution: Thrombin is produced in the liver and is present in the blood as an inactive precursor, prothrombin . It is abundantly expressed in all arterial vessel wall constituents, including endothelial cells, smooth muscle cells, and leukocytes .
Primary Biological Functions: Thrombin’s primary function is to convert fibrinogen into fibrin, forming a blood clot . It also activates other coagulation factors, including factors V, VIII, XI, and XIII . Additionally, thrombin plays a role in platelet activation and aggregation .
Role in Immune Responses and Pathogen Recognition: Thrombin is involved in immune responses by promoting leukocyte recruitment into atherosclerotic plaques and enhancing oxidative stress . It also plays a role in inflammation and angiogenesis .
Mechanisms with Other Molecules and Cells: Thrombin interacts with various molecules and cells through its specific cell membrane receptors, known as protease-activated receptors (PARs), including PAR-1, PAR-3, and PAR-4 . These interactions lead to various cellular responses, including inflammation, cell migration, and proliferation .
Binding Partners and Downstream Signaling Cascades: Thrombin binds to fibrinogen, thrombomodulin, and other coagulation factors through its anion-binding exosites . These interactions trigger downstream signaling cascades that regulate coagulation, inflammation, and cell proliferation .
Regulatory Mechanisms Controlling Expression and Activity: Thrombin activity is regulated by the prothrombinase complex, which includes activated Factor X (Xa) and Factor V (Va) . The presence of calcium ions and phospholipid bilayers also enhances thrombin activity .
Transcriptional Regulation and Post-Translational Modifications: Thrombin is co-translationally modified in a vitamin K-dependent reaction that converts glutamic acids to gamma-carboxyglutamic acid . This modification is essential for its binding to phospholipid surfaces .
Biomedical Research: Thrombin is extensively studied for its role in coagulation and its potential therapeutic applications . It is used in various research models to understand coagulation disorders and develop anticoagulant therapies .
Diagnostic Tools: Thrombin generation assays are used to assess coagulation status in patients with bleeding disorders or thrombotic conditions .
Therapeutic Strategies: Thrombin inhibitors, such as dabigatran, are used as anticoagulant therapies to prevent and treat thromboembolic disorders .