Prepared from homogeneous Human Prothrombin by activation with Human Factor Xa, Human Factor Va and phospholipid. Human Alpha Thrombin purity is determined by SDS-PAGE. Human Alpha Thrombin has a minimum activity of 2,700 NIH units/mg when compared to NIH standard Human Alpha Thrombin.

Prepared as a recombinant protein from serum free stable HEK293 cells. Generated by activation of recombinant human prethrombin II with ecarin. Purified from culture supernatant by heparin affinity chromatography. 

A non-clotting derivative of Thrombin produced from human alpha Thrombin by controlled digest with Trypsin-Sepharose. Gamma Thrombin is a non-coagulant form of Thrombin that retains much of its platelet activating capacity. Gamma Thrombin purity is determined by SDS-PAGE.

Prepared from purified Human Factor VII using Human Factor XIIa. The Factor XIIa is removed using affinity chromagtography. Purity is determined by SDS-PAGE. Human Factor VIIa reduces to 29,500 and 23,500 with the addition of 2-mercaptoethanol. Activity is determined via clotting assay. Factor VIIa, in the presence of calcium ions and the Tissue Factor, activates Factors IX and X to their enzymatically active forms, Factor IXa and Xa.

Activated Protein C (APC) is a serine protease derived from the two chain vitamin K dependent zymogen, Protein C. APC inhibits blood coagulation through the selective inactivation of the cofactors Va and VIIIa. APC is prepared from protein C by activation with purified thrombin. This thrombin is removed after activation by ion exchange chromatography. Activated Protein C purity is determined by SDS-PAGE and shows complete reduction upon incubation with 2-mercaptoethanol.

Prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX in a two step reaction. In the first step an internal Arg-Ala bond is cleaved and in the second step an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce Factor IXa,b.

Human Factor Xa is prepared from homogeneous Human Factor X by activation with Russell's Viper Venom (RVV-X). This RVV-X is removed after activation. Complete activation is observed on 10 % SDS-PAGE gels. Factor Xa as part of the prothrombinase complex along with Factor Va, phospholipids and calcium ions catalyze the rapid conversion of Prothrombin to Thrombin.

Human Factor Xa beta

***NOT AVAILABLE***

Prepared from Human Factor XI using Human Factor XIIa. This XIIa is removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor XIIa and High Molecular Weight Kininogen. During activation by Factor XIIa and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedtly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of vitamin K-dependant blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces.

Human Factor a-XIIa is a serine protease responsible for the activation of Factor XI to XIa in the contact activation system. Human Factor XII and Prekallikrein are thought to be involved in a reciprocal activation mechanism in which XIIa activates Prekallikrein to Kallikrein which in turn converts Factor XII to XIIa. Factor XIIa activates Factor XI to XIa thereby triggering the Contact Factor cascade. Enzyme Research Laboratories offers Factor a-XIIa which is activated by the autoactivation process with Dextran Sulphate and re-purified to remove the activator. The protein purity is determined by SDS-PAGE and activity is determined via clotting assay.

Human Factor XIIa beta.

Prepared from purified Human Factor XIII. Human Factor XIII is cleaved with human alpha thrombin.  The thrombin is subsequently removed via chromatography. 

Activation of Prekallikrein with Factor a-XIIa produces the enzymatically active Kallikrein. Kallikrein is a serine protease which consists of a heavy chain (molecular weight 52,000) and light chains (molecular weights either 36,000 or 33,000) linked by disulphide bridges. Kallikrein possesses enzymatic activity towards Factor XII, High Molecular Weight Kininogen, Plasminogen, Factor XI, Factor IX, Factor VII, prorenin and the complement system. After activation, the activating enzyme Factor XIIa is removed by affinity chromatography. Human Kallikrein purity is determined by SDS-PAGE and shows complete reduction upon incubation with 2-mercaptoethanol.

Prepared from Glu-Plasminogen using urokinase-bound activation column chromatography. Purity is judged by SDS-PAGE. Plasmin is a two chain serine protease linked by 2 disulfide bonds. Among other roles, Plasmin is responsible for the lysis of the fibrin clot, thus producing fibrin degradation products. (FDP's)