Alpha-2-Antiplasmin Polyclonal Antibody – Affinity Purified
Affinity’s Alpha-2-Antiplasmin Polyclonal Antibody – Affinity Purified is the highest level of our a2-Antiplasmin antibody family. During the Antigen Affinity Purification process the IgG has had any non-specific immunoglobulin fraction eliminated which enriches the specificity of the remaining immunoglobulin towards the target antigen. The result is a very high-purity product with a substantially higher titre than whole or purified IgG. Our Alpha-2-Antiplasmin Polyclonal Antibody – Affinity Purified is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v) and is intended for applications such as immunoblotting, immunostaining of cells and several types of immunoassays where the higher signal-to-noise ratio achieved with this enriched product is required.
Product Code: GA2AP-AP
Retail Product Size: 0.5mg vial
Host Animal: Goat Anti-Human a2-Antiplasmin Polyclonal Antibody – Affinity Purified
Species Cross Reactivity: View Chart
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.
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.