A2AP – Alpha 2 Antiplasmin Antibodies
Affinity Biologicals, Inc. manufactures a broad range of A2AP – Alpha 2 Antiplasmin Antibodies which can be found in the listing below. Further information about each individual Alpha 2 Antiplasmin Antibody is available by following the associated links. Our A2AP – Alpha 2 Antiplasmin Antibodies are excellent for use in immunoassays where high sensitivity is required and are frequently the preferred reagent for immunopreciptaion techniques and activity neutralization assays. These antibodies have proven to be extremely useful in the preparation of immune-adsorbent resins for use in immuno-depletion of specific proteins from plasma as well as immuno-affinity purification of proteins. Affinity’s A2AP – Alpha 2 Antiplasmin Antibodies are manufactured for use in research applications.
Listing of Alpha-2-Antiplasmin Antibodies
GA2AP-IG – Goat anti human alpha-2-Antiplasmin, purified IgG (5mg vial)
SA2AP-IG – Sheep anti human A2AP, purified IgG (10mg vial)
GA2AP-HRP – Goat anti human Alpha-2-Antiplasmin, peroxidase conjugated IgG (0.2 mg vial)
GA2AP-AP – Goat anti human Alpah-2-Antiplasmin, affinity purified IgG (0.5 mg vial)
Description of Alpha 2-Antiplasmin
Alpha 2-Antiplasmin (α2AP), also known as Alpha 2-Plasmin Inhibitor (α2PI), 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 α2AP is plasmin, but α2AP also acts as secondary or “backup” inhibitor of activated FXI, activated Protein C and trypsin. Inhibition of these enzymes by α2AP occurs through proteolytic cleavage after Arg364 with subsequent rapid formation of a stable, inactive 1:1 enzyme-α2AP complex. α2AP also acts to regulate fibrinolysis by binding to the lysine binding sites on plasminogen thus competitively inhibiting plasminogen binding to fibrin. About 30% of α2AP present in plasma is partially degraded and lacks a peptide in the carboxyl region that contains the plasminogen-binding site. This form of α2AP (~65 kDa) has a reduced rate of plasmin inhibition and has been referred to as the “slow form” of α2AP. During fibrin formation, a portion of circulating α2AP 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.
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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.