The domain structure of human plasminogen is represented where: K1-K5 = the 5 kringle domains, B-CHAIN = catalytic domain of plasmin , and the arrows indicate the sites of proteolytic cleavage by plasmin, elastase, and plasminogen activators (PA'S).
Price $81.00/500 µg ($74.00/min. 5)
Size 500 µg Formulation 50% glycerol/water (v/v) Storage -20°C Purity >95% by SDS-PAGE Activity Determination Chromogenic assay Shelf Life (properly stored) 12 months
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Size Formulation 50% glycerol/water (v/v) Storage -20°C Purity >95% by SDS-PAGE Activity Determination Chromogenic assay Shelf Life (properly stored) 12 months
Plasminogen (whether Glu-1, Lys-77 or Val-442) is converted to the active serine protease plasmin by hydrolysis of the Arg560-Val561 peptide bond yielding an NH2-terminal heavy (A) chain and a COOH-terminal light (B) chain linked by 2 disulfide bonds (1-3). This conversion is catalyzed by a variety of physiological and pathological activators, including urinary type plasminogen activators, tissue type plasminogen activators, streptokinase, staphylokinase, kallikrein, factors IXa and XIIa. The COOH-terminal derived light chain (Mr=26,000) contains the catalytic triad (His42, Asp85 and Ser180) as well as the streptokinase binding site. The NH2-terminal derived heavy chain ranges in molecular weight from 63,000 to 12,000 depending on the type of plasminogen from which it originated. In the absence of inhibitors, plasmin cleaves the amino-terminal Glu1 to Lys76 peptide from plasmin (plasminogen) to yield Lys-plasmin, which has a greater affinity for fibrin than the Glu form. The heavy chain of Lys-plasminogen contains 5 triple loop disulfide bridged regions of internal sequence homology known as kringles. Kringles 1-4 contain the ω-aminocarboxylic acid and fibrin binding sites.
Plasmin is a serine protease with broad specificity which, in addition to cleavage of fibrin, is capable of activation and/or degradation of compounds of the coagulation, kinin generation and complement systems. Although plasmin can be inhibited by a number of plasma protease inhibitors in vitro, regulation of plasmin in vivo is thought to occur mainly through its interaction with α2-antiplasmin, and to a lesser extent, α2-macroglobulin.
Human Lys-plasmin is prepared from homogeneous Glu-plasminogen using urokinase, as described by Robbins et al. (3). Plasmin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Activity is measured by chromogenic substrate assay and purity is judged by SDS gel electrophoresis.
|Gel||Novex 4-12% Bis-Tris|
|Load||Human Plasmin, 1 µg per lane|
|Standard||SeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64 kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa), Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14 kDa)|
|Mode of action||Enzyme involved in fibrinolysis|
|Molecular weight||83,000 (lys-plasmin) (4)|
|Isoelectric point||6.7-8.3 (3)|
|Structure||Two subunits, Mr=57,000 and Mr=26,000, disulfide linked, 5 kringle domains 22 disulfide bridges, NH2-terminal lysine.|
|Percent carbohydrate||Approximately 2% (2)|
- Robbins, K.C. in Hemostasis and Thrombosis, 2nd edition, ed. R.W. Colman, J. Hirsh, V.J. Marder, E.W. Salzman, pp. 340-357, J.P. Lippincott Co., Philadelphia, 1987.
- Collen, D. in Blood Coagulation, eds. R.F.P. Zwaal and H. C. Hemker, pp. 243-258, Elsevier, New York, (1986).
- Robbins, K.C., Methods in Enzymology, 80, 379 (1981).
- Barlow, G.H., et al., Biochemistry, 23, 2384 (1984).
- Zheng, H., et al., Arthritis Research & Therapy 2009, 11:R93. (Plasmin/Anti-plasmin assay)
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