|Other Names||Plasminogen, Plasmin heavy chain A, Activation peptide, Angiostatin, Plasmin heavy chain A, short form, Plasmin light chain B, PLG|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Secreted. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin Interaction with HRG tethers it to the cell surface|
|Tissue Location||Present in plasma and many other extracellular fluids. It is synthesized in the liver|
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Provided below are standard protocols that you may find useful for product applications.
PLG is a circulating zymogen that is converted to the active enzyme plasmin by cleavage of the peptide bond between arg560 and val561, which is mediated by urokinase and tissue plasminogen activator. The main function of this protein is to dissolve fibrin clots. The protein, like trypsin, belongs to the family of serine proteinases.
Hofmann,S.C., Voith,U. J. Invest. Dermatol. 129 (7), 1730-1739 (2009)Passero,C.J., Mueller,G.M. J. Biol. Chem. 283 (52), 36586-36591 (2008)Ohyama,S., Harada,T. Eur. J. Biochem. 271 (4), 809-820 (2004)Lee,H., Kim,H.K. Arch. Biochem. Biophys. 375 (2), 359-363 (2000)
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