Thrombin, alpha, DFP Active Protein

Thrombin, alpha, DFP, Human

Cat. Num. AAA634672

• Purity: Purified; Human thrombin is prepared from purified prothrombin using a modification of the Lundblad procedure (1) as described by Nesheim et al. (2). Purity is determined by SDS-PAGE analysis and activity is measured in a thrombin specific clotting assa
• Synonyms: Thrombin; alpha; DFP; Human; DFP active protein

• Host: Human plasma
• Purity/Purification: Purified; Human thrombin is prepared from purified prothrombin using a modification of the Lundblad procedure (1) as described by Nesheim et al. (2). Purity is determined by SDS-PAGE analysis and activity is measured in a thrombin specific clotting assa
• Form/Format: Supplied as a liquid in 50% glycerol/H2O. Thrombin is also available with the active site blocked with either DFP, FPRck, or biotinlyated FPRck.

• Specific Activity: ~3800 NIH units/mg
• Extinction Coefficient: E1%1cm, 280nm=18.3 (6)
• Isoelectric Point: 7.0-7.6 (3)
• Mode of Action: Serine protease which cleaves fibrinogen to form fibrin; also responsible for activation of protein C, platelet activation and feedback activation of the procofactors, factor V and factor VIII.
• Structure: Two subunits, ~Mr=6,000 and 31,000
• Percent Carbohydrate: ~5%
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for Thrombin, alpha, DFP active protein

Alpha-thrombin is a highly specific serine protease generated by proteolytic activation of the zymogen prothrombin (1). During coagulation, thrombin cleaves fibrinogen to form fibrin, leading to the ultimate step in coagulation, the formation of a fibrin clot. Thrombin is also responsible for feedback activation of the procofactors factor V and factor VIII. Thrombin has also been reported to activate factor XIII and platelets, and also functions as a vasoconstrictor protein. The procoagulant activity of thrombin is arrested in two ways: 1) inhibition by either heparin cofactor II or the antithrombin III/heparin complex; or 2) complex formation with thrombomodulin. Formation of the thrombin/thrombomodulin complex results in the inability of thrombin to cleave fibrinogen and activate factors V and VIII, but increases the efficiency of thrombin for activation of the anticoagulant, protein C.

Thrombin is a two chain enzyme composed of an NH2-terminal "A" chain (Mr=6,000) and a COOH-terminal "B" chain (Mr=31,000) which remain covalently associated through a single disulfide bond. Human thrombin is 13 amino acids shorter than the bovine thrombin due to a thrombin cleavage site on the human protein that is not present in the bovine protein.
Thrombin is also utilized for site specific cleavage of fusion proteins expressed in bacteria (9-11). A thrombin sensitive site is incorporated between the recombinant protein of interest and peptides or proteins which facilitate purification and/or expression. The target protein is released from the expressed hybrid by cleavage with thrombin. Thrombin can then be easily removed by affinity chromatography.

Product Categories/Family for Thrombin, alpha, DFP active protein

Molecular Biology; MB-Coagulation Factors

NCBI and Uniprot Product Information

• NCBI GI #: 3915685
• Molecular Weight: 36,700
• NCBI Official Full Name: Thrombin-like enzyme flavoxobin

Uniprot Description

Thrombin-like snake venom serine protease that clots fibrinogen (FGA) by releasing fibrinopeptide A. According to PubMed:8585090, only cleaves rabbit fibrinogen, whereas no specificity is described in PubMed:3910643 (tests done on bovine fibrinogen). Also acts as a C3 convertase that independently cleaves human C3 and kick-starts the complement cascade. Also increases urokinase-type plasminogen activator (PLAU) and plasminogen activator inhibitor (SERPINE1) in cultured bovine pulmonary artery endothelial cells. Dose-dependently inhibits collagen-induced platelet aggregation.