Alternative Name(s):

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

Species: (Organism)

Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)

Gene Names:

N/A

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

VIGGDECNINEHRFLVAVYEGTNWTFICGGVLIHPEWVITAEHCARRRMNLVFGMHRKSEKFDDEQERYPKKRYFIRCNKTRTSWDEDIMLIRLNKPVNNSEHIAPLSLPSNPPIVGSDCRVMGWGSINRRIDVLSDEPRCANINLHNFTMCHGLFRKMPKKGRVLCAGDLRGRRDSCNSDSGGPLICNEELHGIVARGPNPCAQPNKPALYTSIYDYRDWVNNVIAGNATCSP

Expression Region:

1-234aa

Subcellular Location:

Secreted

Tissue Specificity:

Expressed by the venom gland.

Protein Length:

Full Length

Pathway:

Mol. Weight:

28.6 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

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.

Research Areas:

Others

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.

Involvement in disease:

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.

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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Peptidase S1 family, Snake venom subfamily

Reference:

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)