SerpinA10 Proteins, Antibodies, cDNA Clones Research Reagents

SERPINA10 (Serpin Family A Member 10) is a protein coding gene located on human chromosome 14q32.13. SERPINA10 is also known as PZI and ZPI. The human SERPINA10 gene encodes a 50707 Da protein containing 444 amino acids. The SERPINA10 protein is restrictedly expressed toward liver. SERPINA10 is related to heparin binding and serine-type endopeptidase inhibitor activity. SERPINA3 is an important paralog of SERPINA10 gene. SERPINA10 is associated with some diseases, including Thrombosis and Protein Z Deficiency.

SerpinA10 Protein (1)

    SerpinA10 Antibody (3)

      SerpinA10 cDNA Clone (26)

      NM_001100607.1
      NM_144834.3

      SerpinA10 Lysate (1)

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        SerpinA10 Background

        Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA1 and ZPI, is a secreted protein that belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA1 / Serpin-A1 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 1 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.

        SerpinA10 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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