Bovine Plasma.
Coagulation factor II, Prothrombin, F2.
Prothrombin bovine native.
Prothrombin, a vitamin K-dependent plasma protein synthesized in the liver, undergoes post-translational modification before being released into the plasma. This modification, facilitated by vitamin K-dependent carboxylase, involves the conversion of ten glutamic acid residues within prothrombin into gamma-carboxyglutamic acid. Notably, prothrombin possesses two kringle regions situated between amino acid residues 40 and 270 of the mature plasma protein. These kringle regions take the place of growth factor domains typically found in various plasma serine proteases.
This product consists of native bovine prothrombin.
The bovine prothrombin is lyophilized without the addition of any other substances.
For reconstitution of the lyophilized bovine prothrombin, sterile 0.9% NaCl is recommended.
Lyophilized bovine prothrombin, while stable at room temperature for up to three weeks, should be stored in a dry environment below -18 degrees Celsius. Once reconstituted, the prothrombin should be stored at 4 degrees Celsius for 2-7 days. For extended storage, storing below -18 degrees Celsius is advised. It is recommended to supplement the prothrombin with a carrier protein, such as 0.1% HSA or BSA, for long-term storage. It is crucial to avoid repeated freeze-thaw cycles.
Coagulation factor II, Prothrombin, F2.
Bovine Plasma.
Prothrombin is a single-chain glycoprotein with a molecular weight of approximately 70,000 Daltons . It consists of several domains, including the Gla domain, two kringle domains, and a serine protease domain. The Gla domain contains gamma-carboxyglutamic acid residues, which are essential for binding calcium ions and interacting with phospholipid surfaces .
Prothrombin is synthesized in the liver and undergoes several post-translational modifications, including gamma-carboxylation of glutamic acid residues in the Gla domain. This modification is vitamin K-dependent and is crucial for the protein’s function. The concentration of prothrombin in normal human plasma is between 5-10 mg/dL .
Activation of prothrombin occurs on the surface of activated platelets and involves the prothrombinase complex, which includes Factor Xa, Factor Va, phospholipids, and calcium ions. This complex cleaves prothrombin at specific sites, resulting in the formation of active thrombin .
Thrombin, the active form of prothrombin, is a serine protease that plays a central role in the coagulation cascade. It converts soluble fibrinogen into insoluble fibrin, forming a stable blood clot. Thrombin also activates other coagulation factors, including Factors V, VIII, and XI, amplifying the coagulation response .
Bovine prothrombin is similar in structure and function to human prothrombin. It is often used in research and industrial applications due to its availability and similarity to human prothrombin. Bovine thrombin, derived from prothrombin, is used in various biochemical assays and as a hemostatic agent in surgical procedures .
Deficiencies or abnormalities in prothrombin can lead to bleeding disorders or thrombotic conditions. For example, prothrombin deficiency, a rare genetic disorder, results in impaired blood clotting and increased bleeding risk. Conversely, elevated levels of prothrombin can increase the risk of thrombosis, leading to conditions such as deep vein thrombosis or pulmonary embolism .