Not available outside of the UK & Ireland.

Application

α2-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

α2-Antiplasmin (α2AP) is an antifibrinolytic protein and an important inhibitor of plasmin. α2AP 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 α2AP 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 α2AP associated with disseminated intravascular coagulation (DIC) and thrombolytic therapy. Elevated levels of α2AP have been reported in a patient with ischemic stroke.

General description

α2-Antiplasmin (α2AP) 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.