Sheep Anti-Human Plasminogen polyclonal antibody for IEP, ELISA. Plasminogen (Pg) is synthesized in the liver and circulates in plasma at a concentration of ~200 ?g/ml (~2.3 ?M). Plasminogen is a single-chain glycoprotein of ~88 kDa that consists of a catalytic domain followed by five kringle structures. Within these kringle structures are four low-affinity lysine binding sites and one high-affinity lysine binding site. It is through these lysine binding sites that plasminogen binds to fibrin and to ?2 Antiplasmin. Native plasminogen (glu-plasminogen) exists in two variants that differ in their extent of glycosylation, and each variant has up to six isoelectric forms with respect to sialic acid content, for a total of 12 molecular forms. Activation of glu-plasminogen by the plasminogen activators urokinase (UPA), or tissue plasminogen activator (tPA) occurs by cleavage after residue Arg560 to produce the two-chain active serine protease plasmin. In a positive feedback reaction, the plasmin generated cleaves an ~8 kDa peptide from glu-plasminogen, producing lys77-plasminogen which has a higher affinity for fibrin and when bound is a preferred substrate for plasminogen activators such as urokinase. Additional activators of plasminogen include kallikrein and activated factor XII. The primary inhibitor of plasmin in plasma is ?2 Antiplasmin. Other physiological inhibitors of plasmin include ?2 macroglobulin and antithrombin.
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