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Thrombin-like enzyme ancrod

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Thrombin-like snake venom serine protease that acts as an anticoagulant. It cleaves fibrinogen (FGA) to split off the A-fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The resulting fibrin polymers are imperfectly formed and much smaller in size (1 to 2 um long) than the fibrin polymers produced by the action of thrombin. These ancrod-induced microthrombi are friable, unstable, urea-soluble and have significantly degraded alpha chains. They do not cross-link to form thrombi. They are markedly susceptible to digestion by plasmin and are rapidly removed from circulation by either reticuloendothelial phagocytosis or normal fibrinolysis, or both. Anticoagulation through the removal of fibrinogen from the blood is rapid, occurring within hours following its administration. It does not activate plasminogen and does not degrade preformed, fully cross-linked thrombin fibrin. It also reduces the level of plasminogen activator inhibitor (PAI) and may stimulate the release of tissue plasminogen activator (PLAT) from the endothelium. The profibrinolytic effect of these 2 actions appears to be limited to local microthrombus degradation.

Below are the list of possible Thrombin-like enzyme ancrod products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Thrombin-like enzyme ancrod

 Thrombin-like enzyme ancrod ELISA Kit
 Thrombin-like enzyme ancrod Recombinant
 Thrombin-like enzyme ancrod Antibody
Also known as Thrombin-like enzyme ancrod (SVTLE) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Venombin A).
Thrombin-like snake venom serine protease that acts as an anticoagu
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lant. It cleaves fibrinogen (FGA) to split off the A-fibrinopeptides (A, AY and AP), but not the B-fibrinopeptide. The resulting fibrin polymers are imperfectly formed and much smaller in size (1 to 2 um long) than the fibrin polymers produced by the action of thrombin. These ancrod-induced microthrombi are friable, unstable, urea-soluble and have significantly degraded alpha chains. They do not cross-link to form thrombi. They are markedly susceptible to digestion by plasmin and are rapidly removed from circulation by either reticuloendothelial phagocytosis or normal fibrinolysis, or both. Anticoagulation through the removal of fibrinogen from the blood is rapid, occurring within hours following its administration. It does not activate plasminogen and does not degrade preformed, fully cross-linked thrombin fibrin. It also reduces the level of plasminogen activator inhibitor (PAI) and may stimulate the release of tissue plasminogen activator (PLAT) from the endothelium. The profibrinolytic effect of these 2 actions appears to be limited to local microthrombus degradation.
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Thrombin-like enzyme ancrod-2

 Thrombin-like enzyme ancrod-2 ELISA Kit
 Thrombin-like enzyme ancrod-2 Recombinant
 Thrombin-like enzyme ancrod-2 Antibody
Also known as Thrombin-like enzyme ancrod-2 (SVTLE) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Venombin A).
Thrombin-like snake venom serine protease. Cleaves fibrinogen (FG
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A) to split of fibrinopeptides AM, AO, and AY; the aberrant fibrinogen is then incapable of being cross-linked, forming easily dispersible clots.
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