Frozen A2AP Deficient Plasma

Product Code:  A2AP-DP

Presentation:  Frozen Alpha-2-Antiplasmin Deficient – Depleted Plasma

Preparation/Handling:  Thaw 1 ml vials in 37oC water bath for 5 minutes; for bulk volumes, thawing time will be dependent on bottle size.

Storage and Stability:  Plasma is shipped frozen and should be stored below -60oC. Product is stable until date stated on vial label when stored at -60oC. Once thawed, plasma is stable for 4 hours at 2-8oC in original vial.

Certificate of Analysis:  available upon request

Lyophilized A2AP Deficient Plasma

Product Code:  A2AP-LDP

Presentation:  Freeze Dried Alpha-2-Antiplasmin Deficient – Depleted Plasma containing 50 mM HEPES and stabalizers.

Reconstitution: Reconstitute with 1 mL of reagent grade water.  Allow contents to dissolve for 15 minutes at room temperature with occasional swirling.  Stability after reconstitution is 4 hours at ambient (18-25oC), or 30 days at –20oC.

Storage and Stability:  Prior to reconstitution, dried plasma should be stored at 2-8°C.  Product is stable until date stated on vial label when stored at 2-8oC.  Stability after reconstitution is 4 hours at ambient (18-25oC), or 30 days at –20oC.

Certificate of Analysis:  available upon request


Description of Alpha 2-Antiplasmin

Alpha 2-Antiplasmin (A2AP), also known as Alpha 2-Plasmin Inhibitor (A2PI), is a member of the SERPIN family of proteinase inhibitors and the primary inhibitor of the enzyme plasmin in blood. It is produced in the liver and circulates in plasma at ~70 μg/ml (~1 μM). α2AP is a single chain molecule with a mass of 67 kDa as determined by SDS-PAGE. The primary target enzyme for A2AP is plasmin, but A2AP also acts as secondary or “backup” inhibitor of activated FXI, activated Protein C and trypsin. Inhibition of these enzymes by A2AP occurs through proteolytic cleavage after Arg364 with subsequent rapid formation of a stable, inactive 1:1 enzyme-α2AP complex. A2AP also acts to regulate fibrinolysis by binding to the lysine binding sites on plasminogen thus competitively inhibiting plasminogen binding to fibrin. About 30% of A2AP present in plasma is partially degraded and lacks a peptide in the carboxyl region that contains the plasminogen-binding site. This form of A2AP (~65 kDa) has a reduced rate of plasmin inhibition and has been referred to as the “slow form” of A2AP. During fibrin formation, a portion of circulating A2AP is cross-linked to the α-chain of fibrin by activated factor XIII, and this linking of plasmin inhibitor to the plasmin substrate provides an additional measure of protection to the fibrin clot from proteolysis by plasmin1-4.

References and Reviews

  1. Aoki N, Suni Y, Miura O, Hirosawa S; Human α2Plasmin Inhibitor; Methods in Enzymology, 223, pp 185-197, 1993.
  2. Shieh BH, Travis J; The Reactive Site of Human α2-Plasmin Inhibitor ; JBC 262, pp 6055-6059, 1987.
  3. Moroi M, Aoki N; Isolation and Characterization of α2-Plasmin Inhibitor from Human Plasma; JBC 251, pp 5956-5965, 1976.
  4. Harpel PC; Blood Proteolytic Enzyme Inhibitors: Their Role in Modulating Blood Coagulation and Fibrinolytic Enzyme Pathways; in Hemostasis and Thrombosis, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 738-747, J.B. Lippincott Co., Philadelphia PA, USA, 1982.

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