Anti-Plasminogen/PLG Antibody Picoband® Fluoro647 Conjugated

Plasmin is an important enzyme present in blood that degrades many blood plasma proteins, including fibrin clots. It is mapped to 6q26. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein is encoded by the PLG gene. The protein encoded by this gene is a secreted blood zymogen that is activated by proteolysis and converted to plasmin and angiostatin. Plasmin dissolves fibrin in blood clots and is an important protease in many other cellular processes while angiostatin inhibits angiogenesis. Defects in this gene are likely a cause of thrombophilia and ligneous conjunctivitis. Two transcript variants encoding different isoforms have been found for this gene.

Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.

1. Forsgren, M., Raden, B., Israelsson, M., Larsson, K., Heden, L.-O. Molecular cloning and characterization of a full-length cDNA clone for human plasminogen. FEBS Lett. 213: 254-260, 1987. 2. Miyata, T., Iwanaga, S., Sakata, Y., Aoki, N. Plasminogen Tochigi: inactive plasmin resulting from replacement of alanine-600 by threonine in the active site. Proc. Nat. Acad. Sci. 79: 6132-6136, 1982.