Specification
| Organism | Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| Expression Host | Yeast |
| Tag Info | N-terminal 6xHis-tagged |
| Purity | Greater than 85% by SDS-PAGE |
| Uniprot ID | P26324 |
| Gene Names | N/A |
| Alternative Names | ; Thrombin-like enzyme ancrod; SVTLE; EC 3.4.21.74; Fibrinogen-clotting enzyme; Snake venom serine protease; SVSP; Venombin A |
| Expression Region | Full Length(1-234aa ) |
| Molecular Weight | 28.6 kDa |
| Protein Sequence | VIGGDECNINEHRFLVAVYEGTNWTFICGGVLIHPEWVITAEHCARRRMNLVFGMHRKSEKFDDEQERYPKKRYFIRCNKTRTSWDEDIMLIRLNKPVNNSEHIAPLSLPSNPPIVGSDCRVMGWGSINRRIDVLSDEPRCANINLHNFTMCHGLFRKMPKKGRVLCAGDLRGRRDSCNSDSGGPLICNEELHGIVARGPNPCAQPNKPALYTSIYDYRDWVNNVIAGNATCSP |
| Form | Liquid or Lyophilization |
| Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. |
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
| 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. |
| Involvement in Disease | |
| Subcellular Location | Secreted |
| Protein Families | Peptidase S1 family, Snake venom subfamily |
| Tissue Specificity | N/A |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |