affinity biologicals/alpha-2-Antiplasmin Polyclonal Antibody/5mg vial/GA2AP-IG

Description

alpha-2-Antiplasmin Polyclonal Antibody

Affinity’s alpha-2-Antiplasmin Polyclonal Antibody is the base level of our alpha-2-Antiplasmin antibody family.  The purity of IgG is typically 90% and is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v).  The titre is essentially the same as the starting antiserum and each vial typically contains the amount of IgG recovered from one milliliter of antiserum.  This alpha-2-Antiplasmin Polyclonal Antibody is generally intended for use in applications such as immuno-precipitation, immuno-electrophoresis, immuno-depletion and activity neutralization assays.

Product Code: GA2AP-IG

Retail Product Size: 5mg vial

Host Animal: Goat Anti-Human alpha-2-Antiplasmin Polyclonal Antibody

Species Cross Reactivity: View Chart

Product Datasheet: Alpha-2-antiplasmin A2AP Polyclonal Antibody, purified anti-human goat IgG

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 plasmin^1-4.

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.