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Alpha-2-Plasmin Inhibitor


a2–plasmin inhibitor and fibrinolysis
The primary physiological inhibitor of plasmin is a2–plasmin inhibitor. The binding of a2 –plasmin inhibitor to plasmin(ogen) plays a critical role in fibrinolysis. The binding of circulating free plasmin(ogen) by a2 –plasmin inhibitor prevents both zymogen and enzyme from binding to fibrin and ultimately initiating fibrinolysis. a2–Plasmin inhibitor already crosslinked to fibrin prevents plasmin catalytic action on local sites of fibrin deposition as well as impeding subsequent activation of plasminogen via plasminogen activator.

  • Price $151.00/100µg ($137.00/min. 5)
    Size 100µg
    Formulation 50 KPO4, 7.5 mM KCl, 75 uM EDTApH 7.4
    Molecular Weight
    Storage -80°C
    Purity >95% by SDS-PAGE
    Compound
    Assay Plasmin inhibition assay
    Shelf Life (properly stored) 12 months
    Chemical Formula
Gel Novex 4-12% Bis-Tris
Load Human α2 –Plasmin Inhibitor, 1 µg per lane
Buffer MOPS
Standard SeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64 kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa), Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14 kDa)

α2 –plasmin inhibitor (α2 -PI) is a single-chain glycoprotein and is one of the major serine proteinase inhibitors circulating in plasma. Physiologically, it is the predominant inhibitor of plasmin and it therefore plays a significant role in the specific inhibition of fibrinolysis. The role of α2 -PI in fibrinolysis is three fold: covalent inhibition of plasmin; interference with the binding of plasminogen to fibrin; and factor XIIIa catalyzed cross-linking of α2-PI to fibrin (1). Rapid inactivation of plasmin proteolytic activity occurs through a two-step process. The inhibitor first forms a reversible complex with plasmin which is sub-sequently followed by the formation of a covalent, enzymatically inactive, complex with the catalytic site in plasmin (2,3). α2-PI also functions by interfering with the binding of plasminogen to fibrin, effectively slowing the activation of plasminogen by fibrin-bound plasminogen activator (4). The interference in binding ultimately delays the initiation of fibrinolysis. Covalent cross-linking of a2-PI to the a-chains of fibrin which is mediated by factor XIIIa, protects crosslinked fibrin clots from plasmin degradation and thereby markedly stabilizes the fibrin clot against fibrinolysis (5). Failure to protect the fibrin clot from rapid dissolution before injured vessels can be restored results in a bleeding tendency described in patients with a deficiency in α2-PI or factor XIII (6,7).

Localization Plasma
Mode of action Inhibits plasmin by forming an irreversible complex with the catalytic active site. Prevents the binding of plasmin to fibrin. Cross-linked by factor XIIIa to fibrin.
Plasma Concentration 69 µg/ml (1)
Molecular weight 58,700 single-chain (determined from amino acid sequence and 14% carbohydrate) and 67,000 (determined by SDS-PAGE) (1)
Extinction coefficient
E
1 %
1 c m, 280 nm
= 14.5 (human) (9)
Isoelectric Point Unknown
Structure Circulates as single chain molecule consisting of 452 amino acids (1).
Percent carbohydrate 14% (w/w) (1)
  1. Aoki, N. et al., Methods Enzymol., 223, 185-197 (1993).
  2. Moroi, M. and Aoki, N., J. Biol. Chem., 251, 5956 (1976).
  3. Wiman, B. and Collen, D., J. Biol. Chem., 254, 9291 (1979).
  4. Moroi, M. and Aoki, N., Thromb. Res., 10, 851 (1977).
  5. Sakata, Y. and Aoki, N., J. Clin. Invest., 69, 536 (1982).
  6. Aoki, N. et al., J. Clin. Invest., 63, 877 (1979).
  7. Israels, E. D. et al., J. Clin. Invest., 52, 2398 (1973).
  8. Holmes, W. E. et al., J. Biol. Chem., 262, 1659 (1987).
  9. Kluft, C. and Los, N., Thromb. Res., 21, 65 (1981).
  10. Tamaki, T. and Aoki, N., J. Biol. Chem., 257, 14767 (1982).
  1. Tseng, I., et al., Am J Physiol Cell Physiol 295:423-431, 2008

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