Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod

• Product Name Alternative:

  ; Thrombin-like enzyme ancrod; SVTLE; EC 3.4.21.74; Fibrinogen-clotting enzyme; Snake venom serine protease; SVSP; Venombin A

• Abbreviation:

  Recombinant Calloselasma rhodostoma Thrombin-like enzyme ancrod protein

• UniProt:

  P26324

• Expression Region:

  1-234aa

• Organism:

  Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)

• Target Sequence:

  VIGGDECNINEHRFLVAVYEGTNWTFICGGVLIHPEWVITAEHCARRRMNLVFGMHRKSEKFDDEQERYPKKRYFIRCNKTRTSWDEDIMLIRLNKPVNNSEHIAPLSLPSNPPIVGSDCRVMGWGSINRRIDVLSDEPRCANINLHNFTMCHGLFRKMPKKGRVLCAGDLRGRRDSCNSDSGGPLICNEELHGIVARGPNPCAQPNKPALYTSIYDYRDWVNNVIAGNATCSP

• Tag:

  N-terminal 6xHis-tagged

• Type:

  In Stock Protein

• Source:

  Yeast

• Field of Research:

  Others

• Relevance:

  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.

• Endotoxin:

  Not test

• Purity:

  Greater than 90% as determined by SDS-PAGE.

• Activity:

  Not Test

• Form:

  Liquid or Lyophilized powder

• Buffer:

  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.

• Reconstitution:

  We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

• Function:

  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.

• Molecular Weight:

  28.6 kDa

• References & Citations:

  Amino acid sequence determination of ancrod, the thrombin-like alpha-fibrinogenase from the venom of Akistrodon rhodostoma.Burkhart W., Simth G.F.H., Su J.-L., Parikh I., Levine H. IIIFEBS Lett. 297:297-301 (1992)

• Storage Conditions:

  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 -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

• Protein Length:

  Full Length