Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod

Others

N/A

VIGGDECNINEHRFLVAVYEGTNWTFICGGVLIHP EWVITAEHCARRRMNLVFGMHRKSEKFDDEQERYP KKRYFIRCNKTRTSWDEDIMLIRLNKPVNNSEHIA PLSLPSNPPIVGSDCRVMGWGSINRRIDVLSDEPR CANINLHNFTMCHGLFRKMPKKGRVLCAGDLRGRR DSCNSDSGGPLICNEELHGIVARGPNPCAQPNKPA LYTSIYDYRDWVNNVIAGNATCSP

Full Length

N-terminal 6xHis-tagged

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 roved from circulation by either reticuloendothelial phagocytosis or normal fibrinolysis, or both. Anticoagulation through the roval 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.

Greater than 90% as determined by SDS-PAGE.

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.

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.

Peptidase S1 family, Snake venom subfamily