|Related Categories||3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Blood,|
|form||aqueous glycerol solution|
|shipped in||wet ice|
|Gene Information||cow ... F10(280787)|
One unit of activated Factor X will liberate 1.0 μmole of p-nitroanilide from N-benzoyl-
Fusion proteins are commonly expressed with a factor Xa cleavable Ile-Glu (or Asp)-Gly-Arg-↓-X sequence. Typically 1 mg of fusion protein can be incubated with 10 μg of factor Xa for 2.5 hours at 37 °C.
Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin.
The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X.
It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence.
pH Optimum: 7.6-8.0
Temperature Optimum: 37 °C
Factor Xa is a serine endoproteinase and a member of the S1 peptidase family. Factor Xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. Factor Xa′s prothrombin conversion activity is greatly enhanced in vivo when complexed with factor V, calcium ions and phospholipids on the activated platelet surface.
The zymogen form, Factor X, is activated in vivo by two different pathways. The intrinsic pathway utilizes a catalytic complex composed of factor IXa, factor VIII, phospholipids and calcium ions. The extrinsic pathway utilizes a complex of factor VII and tissue factor. The factor X zymogen is a 55 KDa glycoprotein with a light and heavy chain joined by a single disulfide.
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Rivaroxaban, a direct inhibitor of the coagulation factor Xa interferes with hormonal-induced physiological modulations in human female osteoblastic cell line SaSO2. Somjen D, Katzburg S, Gigi R, et al. J. Steroid Biochem. Mol. Biol. 135, 67-70, (2013)
Outcomes of discontinuing rivaroxaban compared with warfarin in patients with nonvalvular atrial fibrillation: analysis from the ROCKET AF trial (Rivaroxaban Once-Daily, Oral, Direct Factor Xa Inhibition Compared With Vitamin K Antagonism for Prevention of Stroke and Embolism Trial in Atrial Fibrillation). Patel MR, Hellkamp AS, Lokhnygina Y, et al. J. Am. Coll. Cardiol. 61(6), 651-8, (2013)
Rivaroxaban in patients stabilized after a ST-segment elevation myocardial infarction: results from the ATLAS ACS-2-TIMI-51 trial (Anti-Xa Therapy to Lower Cardiovascular Events in Addition to Standard Therapy in Subjects with Acute Coronary Syndrome-Thrombolysis In Myocardial Infarction-51). Mega JL, Braunwald E, Murphy SA, et al. J. Am. Coll. Cardiol. 61(18), 1853-9, (2013)
Active-site mapping of bovine and human blood coagulation serine proteases using synthetic peptide 4-nitroanilide and thio ester substrates. Cho K, Tanaka T, Cook RR, et al. Biochemistry 23(4), 644-50, (1984)
Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. McMullen BA, Fujikawa K, Kisiel W, et al. Biochemistry 22(12), 2875-84, (1983)
Enzymatic Cleavage of Fusion Proteins with Factor Xa. La Vallie, E.R., and McCoy, J.M., Ausubel, F.M., ed. Curr. Protoc. Mol. Biol., (1994) 2, 16.4.6-16.4.7
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