Human Serpin A10/ZPI Antibody

  
  • Species Reactivity
    Human
  • Specificity
    Detects human Serpin A10/ZPI in direct ELISAs and Western blots.
  • Source
    Monoclonal Mouse IgG2B Clone # 895910
  • Purification
    Protein A or G purified from hybridoma culture supernatant
  • Immunogen
    Chinese hamster ovary cell line CHO-derived recombinant human Serpin-A10/ZPI
    Met1-Leu444
    Accession # Q9UK55
  • Formulation
    Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
  • Label
    Unconjugated
Applications
  •  
    Recommended
    Concentration
    Sample
  • Western Blot
    1 µg/mL
    See below
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Data Examples
Detection of Human Serpin A10/ZPI by Western Blot. Western blot shows conditioned media of NS0 mouse myeloma cell line either mock transfected or transfected with human Serpin A10. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human Serpin A10/ZPI Monoclonal Antibody (Catalog # MAB8115) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific bands were detected for Serpin A10/
ZPI at approximately 70-75 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
  • Reconstitution
    Reconstitute at 0.5 mg/mL in sterile PBS.
  • Shipping
    The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
  • Stability & Storage
    Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
    • 12 months from date of receipt, -20 to -70 °C as supplied.
    • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
    • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Serpin A10/ZPI

Protein Z-dependent Protease Inhibitor (ZPI), also known as SerpinA10 (SERine Proteinase INhibitor-clade A10) is a monomeric, secreted member of the A (or extracellular) clade within the serpin superfamily of protease inhibitors (1-4).  In general, members of this superfamily regulate multiple proteolytic cascades, and are particularly effective due to the fact that their inhibitory activities can be fine-tuned through the participation of discrete, non-serpin co-factors (4). Serpins are unusual in that they are one-time use, non-recyclable proteins whose native state is thermodynamically unstable. They act as non-physiologic substrates for enzymes that, once cleaved, form a covalent bond with the target enzyme, rendering it inactive (1, 2). ZPI is a hepatocyte-derived glycoprotein associated with the coagulation cascade (3, 5-7). Following vessel damage, underlying support collagen and fibroblasts are exposed to circulating plasma and platelets. This results in the activation of two coagulation pathways; an intrinsic pathway involving platelets, and an extrinsic pathway involving vascular stromal cells. Both pathways converge at the activation step for factor X, which converts prothrombin into thrombin, a prelude to the generation of fibrin. ZPI negatively regulates the activation state of two coagulation factor enzymes; factor XIa and factor Xa (5-7). Factor XI is unique to the intrinsic pathway, while factor X, as noted, is common to both pathways. Inhibition is most efficiently accomplished by ZPI binding to either factor Xa (with protein Z [PZ], calcium and phospholipids) or XIa (lacking non-heparin co‑factors), precluding them from activating downstream zymogens. Binding is accompanied by serpin cleavage, but unlike a typical serpin, ZPI does not stay bound to enzyme; rather, it dissociates into a 4 kDa C-terminal fragment and a 68 kDa N-terminal sequence (6, 8, 9). Following dissociation, a second ZPI molecule is recruited, and the process repeated. In humans, the majority of ZPI circulates in a complex with PZ. PZ serves as an intermediary, bringing ZPI in contact with factor Xa or XIa on the surface of platelets (1, 10-12). Once cleaved, ZPI dissociates from PZ, and PZ is free to bind and present additional ZPI to Xa and XIa. Cell-surface heparan sulfate on endothelium is also reported to act as a scaffold for ZPI:Xa interactions (8, 13).  Human and mouse systems are not strictly analogous, as ZPI > PZ in human blood, while PZ>ZPI in mouse blood (11). Mature human ZPI is 423 amino acids (aa) in length (aa 22-444), and it contains a factor Xa cleavage site between Tyr408Ser409. Human and mouse ZPI share 71% aa sequence identity. Notably on SDS-PAGE, human ZPI runs about 72 kDa, while mouse and rat ZPI exhibit MWs of 91 kDa and 51 kDa, respectively (14).     

  • References:
    1. Chen, H. et al. (2013) Cardiovasc. Haematol. Disord. Drug Targets 13:99.
    2. Law, R.H.P. et al. (2006) Genome Biol. 7:216.
    3. Han, X. et al. (1999) Biochemistry 38:11073.
    4. Corral, J. et al. (2007) Br. J. Haematol. 137:99.
    5. Han, X. et al. (1998) Proc. Natl. Acad. Sci. USA 95:9250.
    6. Han, X. et al. (2000) Blood 96:3049.
    7. Broze, G.J. et al. (2001) Thromb. Haemost. 86:8.
    8. Vasse, M. (2011) Hamostaseologie 31:155.
    9. Huang, X. et al. (2012) Blood 120:1726.
    10. Huang, X. et al. (2010) J. Biol. Chem. 285:20399.
    11. Girard, T.J. et al. (2013) J. Thromb. Haemost. 11:375.
    12. Wei, Z. et al. (2009) Blood 114:3662.
    13. Huang, X. et al. (2011) J. Biol. Chem. 286:8740.
    14. Zhang, J. & G.J. Broze (2001) Thromb. Haemost. 85:861.
  • Long Name:
    Serpin Peptidase Inhibitor, Clade A, Member 10
  • Entrez Gene IDs:
    51156 (Human); 217847 (Mouse); 171154 (Rat)
  • Alternate Names:
    antitrypsin), member 10; member 10; PZI; PZIprotein Z-dependent protease inhibitor; serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase; Serpin A10; serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin); ZPI; ZPIPZ-dependent protease inhibitor
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