?2-Antiplasmin from human plasma has been used as a protease inhibitor to treat human microvascular endothelial cells (HMEC-1) and demonstrate the role of factors responsible for endothelial cells detachment. It has also been used to study its effect on the release of proteolytic activity under reducing conditions in therapeutic human serum albumin-containing products with a new neoepitope endopeptidase immunoassay.
Biochem/physiol Actions
?2-Antiplasmin (?2AP) is an antifibrinolytic protein and an important inhibitor of plasmin. ?2AP mediates clot formation by covalently cross-linking with the glutamine and the lysine residue of fibrin clot via activated factor XIII (FXIIIa). This prevents the clot from extreme degradation by plasmin. An inborn insufficiency of ?2AP results in an autosomal recessive condition leading to a rare bleeding disorder. The severity of the bleeding condition is defined by the individual?s genetic variation. Studies show lower levels of ?2AP associated with disseminated intravascular coagulation (DIC) and thrombolytic therapy. Elevated levels of ?2AP have been reported in a patient with ischemic stroke.
General description
?2-Antiplasmin (?2AP) is a glycoprotein and a member of the serine protease inhibitor (serpin) family. The protein is mainly synthesized in the liver and found in the kidney and brain. The serpin peptidase inhibitor, clade F member 2 (SERPINF2) gene is mapped to human chromosome 17p13.3.
Physical form
Lyophilized powder containing Bis-tris buffer and NaCl.
Unit Definition
One unit will reduce the activity of two units of plasmin by 50% at 37 °C, pH 7.2, using Val-Leu-Lys-p-nitroanilide.