ALPHA 2 ANTIPLASMINHUMAN PLASMA

Biochem/physiol Actions

α-2 antiplasmin (AAP) is the primary physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots. It inhibits the action of protease by the formation In addition to plasmin, it is also an efficient inhibitor of trypsin and chymotrypsin. α-antiplasmin-deficiency is a rare coagulation disorder which allows unrestrained fibrinolytic activity. AAP is known to inhibit fibrinogenolysis by preventing free plasmin circulation.

α-2 antiplasmin (AAP) is the primary physiological inhibitor of the serine protease plasmin, which is responsible for the dissolution of fibrin clots. In addition to plasmin, it is also an efficient inhibitor of trypsin and chymotrypsin. α-antiplasmin-deficiency is a rare coagulation disorder which allows unrestrained fibrinolytic activity. Individuals with this condition may receive therapeutic A2AP prior to surgery to prevent postoperative hemorrhaging.

General description

α-2 antiplasmin (AAP) is a member of the Serpin superfamily. Liver and kidney are major sites of its production and other tissues such as muscle, intestine, central nervous system, and placenta also express its mRNA at a moderate level. The tissue expression pattern indicates that it is a key regulator of plasmin mediated proteolysis in these tissues. The AAP gene is mapped to human chromosome 17p13 and codes for a glycoprotein of single chain containing 464 amino acid residues.

α-2 antiplasmin (AAP) is a member of the Serpin superfamily. Liver and kidney are major sites of its production and other tissues such as muscle, intestine, central nervous system, and placenta also express its mRNA at a moderate level. The tissue expression pattern indicates that it is a key regulator of plasmin mediated proteolysis in these tissues. The gene encoding this protein is localized on human chromosome 17.

Physical form

Lyophilized from 20 mM Bis-Tris, pH 6.4, with 200 mM NaCl.

Reconstitution

In water or aqueous buffer