一般描述
Factor V is a single chain glycoprotein involved in the blood coagulation cascade. It is the procofactor of Va which accelerates the conversion of prothrombin to thrombin.
应用
Factor V is a key component in blood coagulation systems, where deficiencies can inhibit thrombin generation and affect hemostasis. It has been used in studies of Coagulopathic bleeding which occurs following injury and is a leading cause of in hospital deaths.
外形
Aqueous solution containing 50% (v/v) glycerol
其他说明
One unit is equivalent to the Factor V activity in 1.0 mL of normal human plasma at pH 7.4 at 37 °C.
View this factors role in the Coagulation Cascade.
免责声明
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
储存分类代码
10 - Combustible liquids
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
高风险级别生物产品--人源产品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Early coagulopathy in trauma patients: An on-scene and hospital admission study.
Floccard B., et al.
Injury (2010)
Sandro B Rizoli et al.
The Journal of trauma, 71(5 Suppl 1), S427-S434 (2011-12-17)
Coagulopathic bleeding is a leading cause of in-hospital death after injury. A recently proposed transfusion strategy calls for early and aggressive frozen plasma transfusion to bleeding trauma patients, thus addressing trauma-associated coagulopathy (TAC) by transfusing clotting factors (CFs). This strategy
Eliza A Ruben et al.
Blood, 137(22), 3137-3144 (2021-03-09)
Coagulation factor V (fV) is the precursor of fVa, which, together with fXa, Ca2+, and phospholipids, defines the prothrombinase complex and activates prothrombin in the penultimate step of the coagulation cascade. We solved the cryogenic electron microscopy (cryo-EM) structures of
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