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Alpha 2 Antiplasmin

16-16-012901
Athens Research
Protein IDP08697
Product group Proteins / Signaling Molecules
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Overview

  • Supplier
    Athens Research
  • Product Name
    Alpha 2 Antiplasmin
  • Delivery Days Customer
    9
  • Applications Supplier
    Proteolytic Inhibition, Fibrinolysis, Coagulation, In Vitro Diagnostic Testing
  • Certification
    Research Use Only
  • Estimated Purity
    ≥95% by SDS-PAGE
  • Protein IDP08697
  • Protein Name
    Alpha-2-antiplasmin
  • Scientific Description
    Alpha-2 antiplasmin (alfa2AP) is a key serine protease inhibitor found in plasma at approximately 70 ug/mL, primarily synthesized by the liver. Its main function is to regulate fibrinolysis by rapidly and efficiently inhibiting plasmin, the enzyme responsible for breaking down fibrin clots. By binding to plasmin and preventing its activity, alfa2AP stabilizes blood clots and prevents excessive bleeding. It also interferes with plasminogen binding to fibrin and becomes cross-linked to fibrin during clot formation, further enhancing clot stability. Deficiency of alfa2AP is a rare inherited coagulation disorder that results in unrestrained plasmin activity and excessive fibrinolysis, leading to a significant risk of spontaneous or postoperative bleeding. This condition may present as severe bleeding episodes, particularly after trauma or surgery. Therapeutically, antifibrinolytic agents such as aminocaproic acid or tranexamic acid are commonly administered to patients with alfa2AP deficiency to prevent or control bleeding, especially in surgical settings. Beyond bleeding disorders, elevated alfa2AP levels are linked to increased risk and poor outcomes in cardiovascular diseases, including deep vein thrombosis and ischemic stroke, making it a potential therapeutic target in these conditions.
  • Shelf life instruction
    more then 1 year
  • Source
    Source human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
  • Storage Instruction
    ≤ -20°C
  • UNSPSC
    41116100

References

  • Singh, S., et al., (2017), 'Releasing the Brakes on the Fibrinolytic System in Pulmonary Emboli: Unique Effects of Plasminogen Activation and alfa2-Antiplasmin Inactivation', Circulation, 135: pp 1011–1020.
    Read this paper
  • Singh, S., et al., (2019), 'Venous stasis-induced fibrinolysis prevents thrombosis in mice: role of a2-antiplasmin', Blood, 134(12): pp 970-978.
    Read this paper
  • Pechlivani, N., et al., (2025), 'Use of Affimer technology for inhibition of alfa2-antiplasmin and enhancement of fibrinolysis', Blood Adv, 9(1): pp 89–100.
    Read this paper
  • Tivawala, R., et al., (2021), 'The role of SERPIN citrullination in thrombosis', Cell Chemical Biology 28(12): pp 1728-1739.e5.
    Read this paper
  • Sochaj-Gregorczyk, A., et al., (2020), 'Plasmin inhibition by bacterial serpin: Implications in gum disease', The FASEB Journal, 34: pp 619–630.
    Read this paper