Bovine Thrombin was derived from bovine plasma and lungs from US sourced animals under 30 months of age. The cattle are ante and post mortem inspected by a U.S. Veterinary Service Inspector where they were apparently free from infectious and contagious diseases. All donor animals were born and sourced from herds in a U.S. geographical area where Bovine Spongiform Encephalopathy has not been detected. All animals used were from a natural beef program in accordance to FDA Regulation 21 CFR 589.2000 which prohibits the use of animal proteins in ruminant feeds.
Salt Environment: Glycine, Sodium Chloride, Calcium Chloride
Recommended diluent for reconstitution: 0.9% NaCl
This product is for in vitro (diagnostic) use only. Not for human or animal consumption.
The technical grade bovine thrombin (90 - 250 U/mg protein) is used by many diagnostic companies worldwide to defibrinate plasma, producing serum matrixes to be used as controls and standards or in polyclonal antibody production. Using bovine thrombin in polyclonal antibody production to defibrinate plasma may increase antibody yields by 15-20% over off-the-clot methods of defibrination.
规格
产品名称
工业级牛凝血酶
英文别名
fibrinogenase | Factor IIa | F2 | coagulation factor II
规格或纯度
EnzymoPure™, 50,000 - 150,000 units/g powder
生化机理
Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (By similarity). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (By similarity). Miscellaneous: Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa. Catalytic activity: Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. Activity regulation: Activity is promoted in the presence of negatively charged surfaces, such as polyphosphate and dextran sulfate (By similarity). Inhibited by SERPINA5 (By similarity).
Post-translational: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. In the penultimate step of the coagulation cascade, prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa (F10), cofactor Va (F5), and phospholipids. This activation requires factor Xa-catalyzed sequential cleavage at 2 sites, Arg-317 and Arg-366, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-317, leading to the formation of the inactive intermediate prethrombin-2. This pathway preferentially occurs on platelets and in the absence of cofactor Va. In the second pathway, the first cleavage occurs at Arg-366, which separates protease domain into 2 chains that remain connected through a disulfide bond and generates the active intermediate meizothrombin. The presence of cofactor Va directs activation along the meizothrombin pathway and greatly accelerates the rate of cleavage at Arg-366, but has a smaller effect on the cleavage of meizothrombin at Arg-317. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells.
生物活性
50,000 - 150,000 U/g enzyme powder; 90-250 U/mg protein
I2607007
危险品化学品经营许可证（带存储）