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Human Alpha 2 Antiplasmin
Native biologically active whole molecule
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Proteins Synonyms: A2AP, Alpha-2-plasmin inhibitor (Alpha-2-PI), Serpin F2, AAP, PLI, Alpha-2-AP, α2AP Biological Activity: ≥ 5.0 U/mg Source: Human Plasma Purity: ≥ 95% by SDS-PAGE Physical State: Lyophilized from 20 mM Bis-Tris, pH 6.4, with 200 mM NaCl. Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
A2AP, Alpha-2-plasmin inhibitor (Alpha-2-PI), Serpin F2, AAP, PLI, Alpha-2-AP, α2AP
Description of Human Alpha 2 Antiplasmin
Human Alpha 2 Antiplasmin is a 70 kDa protein. Alpha-2 antiplasmin (α2AP) is a key serine protease inhibitor found in plasma at approximately 70 µg/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, α2AP 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 α2AP 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 α2AP deficiency to prevent or control bleeding, especially in surgical settings. Beyond bleeding disorders, elevated α2AP 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.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Biological Activity
≥ 5.0 U/mg
Storage
For long term, store Human Alpha 2 Antiplasmin at ≤ -20°C.
Applications
Proteolytic Inhibition, Fibrinolysis, Coagulation, In Vitro Diagnostic Testing.
Citations/Publications
Singh, S., et al., (2017), 'Releasing the Brakes on the Fibrinolytic System in Pulmonary Emboli: Unique Effects of Plasminogen Activation and α2-Antiplasmin Inactivation', Circulation, 135: pp 1011–1020. Available at DOI: 10.1161/CIRCULATIONAHA.116.024421
Singh, S., et al., (2019), 'Venous stasis-induced fibrinolysis prevents thrombosis in mice: role of a2-antiplasmin', Blood, 134(12): pp 970-978. Available at DOI 10.1182/blood.2019000049
Pechlivani, N., et al., (2025), 'Use of Affimer technology for inhibition of α2-antiplasmin and enhancement of fibrinolysis', Blood Adv, 9(1): pp 89–100. Available at https://doi.org/10.1182/bloodadvances.2024014235
Tivawala, R., et al., (2021), 'The role of SERPIN citrullination in thrombosis', Cell Chemical Biology 28(12): pp 1728-1739.e5. Available at: https://doi.org/10.1016/j.chembiol.2021.07.009
Sochaj-Gregorczyk, A., et al., (2020), 'Plasmin inhibition by bacterial serpin: Implications in gum disease', The FASEB Journal, 34: pp 619–630. Available at DOI: 10.1096/fj.201901490RR.
NCBI: https://www.ncbi.nlm.nih.gov/protein/P08697
Shipped with ice packs
Gel Scan of Human Alpha 2 Antiplasmin
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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