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  • Anti-SerpinA10 antibody

Anti-SerpinA10 antibody

Cat.#: 142382

Special Price 145.0 USD

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Product Information

  • Product Name
    Anti-SerpinA10 antibody
  • Documents
  • Description
    Rabbit Polyclonal to Mouse SerpinA10
  • Tested applications
    ELISA
  • Species reactivity
    Mouse SerpinA10
  • Alternative names
    ZPI antibody; ZPI antibody; MGC25863 antibody; PZI antibody; PZI antibody; Serpina10 antibody; SerpinA10 antibody; UNQ707/PRO1358 antibody; PZI antibody; ZPI antibody; PZI antibody; ZPI antibody
  • Immunogen
  • Isotype
    Rabbit IgG
  • Preparation
    Produced in rabbits immunized with purified, recombinant Mouse SerpinA10 . SerpinA10 specific IgG was purified by Mouse SerpinA10 affinity chromatography.
  • Clonality
    Polyclonal
  • Formulation
    0.2 μm filtered solution in PBS
  • Storage instructions
    This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
    Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
  • Applications

    ELISA: 0.1-0.2 μg/ml

    This antibody can be used at 0.1-0.2 μg/ml with the appropriate secondary reagents to detect Mouse SerpinA10.

  • Validations
  • Background
    Mouse 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.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"