α-2 antiplasmin Anticuerpo(P-19): sc-67511

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The serine proteinase inhibitors (serpins) comprise a superfamily of proteins with a diverse set of functions, including the control of blood coagulation, complement activation, programmed cell death and development. Serpins are secreted glycoproteins that contain a stretch of peptide that mimics a true substrate for a corresponding serine protease. Alpha-2 antiplasmin (also referred to as Alpha-2-AP or Alpha-2-plasmin inhibitor) is a member of the serpin family that inhibits plasmin. It is the most potent and rapidly acting of the plasmin inhibitors and is thought to play a key role in the regulation of fibrinolysis and degradation of various other proteins. Alpha-2 antiplasmin interferes with the binding of plasminogen to fibrin because lysine residues in its carboxy-terminal region compete with those in fibrin. As plasmin degrades blood clots, impaired activity of Alpha-2 antiplasmin leads to a bleeding tendency.