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Human SerpinA10 Gene ORF cDNA clone expression plasmid, N-HA tag

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Expression host: Human Cells  
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50315-M08H-20
50315-M08H-100
20 µg 
100 µg 
Add to Cart
Reactivity: Mouse  
Application: ELISA  
    50315-RP02-50
    50315-RP02-200
    50315-RP02-100
    50 µg 
    200 µg 
    100 µg 
    Add to Cart
    Reactivity: Mouse  
    Application: ELISA  
      50315-T16-50
      50315-T16-200
      50315-T16-100
      50 µg 
      200 µg 
      100 µg 
      Add to Cart
      Reactivity: Mouse  
      Application: ELISA  
        50315-RP01-400
        50315-RP01-200
        50315-RP01-100
        400 µg 
        200 µg 
        100 µg 
        Add to Cart

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        SerpinA10 cdna-clone Background

        Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA10 and ZPI, is a secreted protein which belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA10 / Serpin-A10 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors).Over 1000 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.

        Human SerpinA10 cdna-clone References
      • Han X, et al., 1998, Proc Natl Acad Sci. USA  95: 9250-5.
      • Han X, et al., 2000, Blood 96: 3049-55.
      • Irving JA, et al.,2000, Genome Res. 10 (12): 1845-64.
      • Irving J, et al.,2002, Mol Biol Evol. 19 (11): 1881-90.
      • Rawlings ND, et al.,2004, Biochem J. 378 (Pt 3): 705-16.
      • Water N, et al., 2004, Br J Haematol. 127:190-4.
      • Wei Z, et al., 2009, Blood 114 (17): 3662-7.
      • Whisstock JC, et al.,2010, J Biol Chem. 285 (32): 24307-12.
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