Thrombin Bovine
Coagulation Factor II (Thrombin), Prepro-Coagulation Factor II, EC 3.4.21.5, RPRGL2, THPH1, Coagulation Factor II, Prothrombin B-Chain, Serine Protease, Prothrombin, EC 3.4.21, PT, F2.
Sterile Filtered beige lyophilized (freeze-dried) powder.
Description
Product Specs
Thrombin, also known as activated Factor IIa, is a crucial enzyme in the coagulation cascade. It drives the conversion of soluble fibrinogen into insoluble fibrin strands, which form the basis of blood clots. As a serine protease (EC 3.4.21.5), thrombin catalyzes multiple reactions in the coagulation pathway. Its actions include the activation of factors XI, V, VIII, and XIII. Furthermore, thrombin interacts with protease-activated receptors on platelets, leading to their activation. The high specificity of thrombin has made it a valuable tool in biochemistry. Its cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is frequently incorporated into linker regions of recombinant fusion protein constructs. This allows for the efficient removal of purification tags from the target protein after purification, as thrombin cleaves specifically between the Arginine and Glycine residues of this sequence.
Sterile Filtered, lyophilized powder with a beige color.
The lyophilized thrombin is formulated with glycine, calcium chloride (CaCl2), and sodium chloride (NaCl) at a pH of 6.8.
For reconstitution of the lyophilized thrombin, 0.9% sodium chloride (NaCl) solution is recommended.
The biological activity of this thrombin is 164 US units per milligram of protein.
Lyophilized thrombin, while stable at room temperature for up to three weeks, should ideally be stored in a dry environment below -18 degrees Celsius. Once reconstituted, thrombin can be stored at 4 degrees Celsius for 2-7 days. For extended storage, freezing at -18 degrees Celsius is recommended. To enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. Avoid repeated freeze-thaw cycles to maintain product integrity.
Coagulation Factor II (Thrombin), Prepro-Coagulation Factor II, EC 3.4.21.5, RPRGL2, THPH1, Coagulation Factor II, Prothrombin B-Chain, Serine Protease, Prothrombin, EC 3.4.21, PT, F2.
Product Science Overview
Bovine thrombin is produced from its precursor, prothrombin, through enzymatic cleavage by activated Factor X (Xa) in the presence of calcium ions and phospholipids . The active form of thrombin consists of two chains: a light chain (A chain) and a heavy chain (B chain), connected by a disulfide bond . The B chain contains carbohydrate portions with N-linked glycosylation .
Thrombin’s primary function is to convert soluble fibrinogen into insoluble fibrin, which forms the meshwork of a blood clot . It also activates other coagulation factors, such as Factor V, Factor VIII, and Factor XIII, amplifying the coagulation cascade . Additionally, thrombin has roles in platelet activation and aggregation, further contributing to hemostasis .
Thrombin cleaves fibrinogen at specific arginine residues, releasing fibrinopeptides A and B and forming fibrin monomers . These monomers polymerize to form a fibrin clot, which is stabilized by Factor XIIIa through the formation of covalent cross-links . Thrombin also interacts with thrombomodulin, a cofactor that modulates its activity to activate protein C, an anticoagulant .
