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Mouse Coagulation Factor XI/F11 Gene ORF cDNA clone expression plasmid, C-His tag

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Description: Active  
Expression host: Human Cells  
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10302-H08H-50
10302-H08H-20
10302-H08H-10
50 µg 
20 µg 
10 µg 
Add to Cart
Reactivity: Human  
Application: 
    10302-T16-50
    10302-T16-200
    10302-T16-100
    50 µg 
    200 µg 
    100 µg 
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    Reactivity: Human  
    Application: ELISA  
      10302-MM04-50
      10302-MM04-200
      10302-MM04-100
      50 µg 
      200 µg 
      100 µg 
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      Reactivity: Human  
      Application: ELISA  
        10302-R007-50
        10302-R007-100
        50 µg 
        100 µg 
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        Reactivity: Human  
        Application: ELISA  
          10302-RP01-400
          10302-RP01-200
          10302-RP01-100
          400 µg 
          200 µg 
          100 µg 
          Add to Cart
          Reactivity: Human  
          Application: ELISA  
            10302-RP02-50
            10302-RP02-200
            10302-RP02-100
            50 µg 
            200 µg 
            100 µg 
            Add to Cart

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            Coagulation Factor XI/F11 cdna-clone Background

            Factor XI (plasma thromboplastin antecedent) is a plasma glycoprotein, and a zymogen acting as a serine protease which participates in blood coagulation as a catalyst in the conversion of factor IX to factor IXa in the presence of calcium ions. It is an unusual dimeric protease, with structural features that distinguish it from vitamin K-dependent coagulation proteases. The factor XI is synthesized in the liver as a single polypeptide chain with a molecular weight estimated between 125 ~160 kDa and then is processed into a disulfide-bond linked homodimer. FXI is a homodimer, with each subunit containing four apple domains and a protease domain. The apple domains form a disk structure with binding sites for platelets, high molecular weight kininogen, and the substrate factor IX (FIX). FXI is converted to the active protease FXIa by cleavage of the Arg369-Ile370 bond on each subunit. After the activation reaction, Factor XIa is composed of two heavy and two light chains held together by three disulfide bonds. The heavy chains are derived from the amino termini of the zymogen and responsible for the binding of factor XI to high molecular weight kininogen and for the activation of factor IX, while the light chain contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases. FXI deficiency is a disorder characterized by a mild or no bleeding tendency. Severe FXI deficiency is an injury-related bleeding disorder common in Ashkenazi Jews and rare worldwide.

            Mouse Coagulation Factor XI/F11 cdna-clone References
          • Gailani D, et al. (2009) Structural and functional features of factor XI. J Thromb Haemost. 7 Suppl 1: 75-8.
          • Duga S, et al. (2009) Factor XI Deficiency. Semin Thromb Hemost. 35(4): 416-25.
          • Emsley J, et al. (2010) Structure and function of factor XI. Blood. 115(13): 2569-77.
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