The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
0% on D-VLK chromogenic plasmin substrate.
% SDS-PAGE. ab92799 is prepared from Lys plasmin by active site-specific inactivation with a molar excess of Phe-Pro-Arg chloromethyl ketone, followed by extensive dialysis to remove free inhibitor.
Activity: 0% on D-VLK chromogenic plasmin substrate.
Solubility: > 2 mg/mL and < 5 mg/mL
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Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Plasmin is an enzyme formed in the circulating blood, and many other extracellular fluids, from the zymogen plasminogen. Plasminogen is a single-chain glycoprotein with 790 amino acid residues. Activation to the active form, plasmin, by urokinase involves cleavage at the arg-val bond between residues 560 and 561, resulting in the formation of the 2-chain plasmin molecule held together by 2 disulfide linkages. The heavier chain contains about 411 residues and the lighter chain about 233. The main function of plasmin is the digestion of fibrin in blood clots. Plasmin is a proteolytic enzyme with a specificity similar to that of trypsin. Like trypsin, plasmin belongs to the family of serine proteinases, in which the active site catalytic triad, his-57, asp-102, and ser-195 (chymotrypsin numbering), is situated in the light chain.
Plasmin acts as a proteolytic factor in a variety of processes other than fibrinolysis; including embryonic development, tissue remodelling, tumour invasion and inflammation; in ovulation it weakens the walls of the Graafian follicle. A Deficiency of plasmin may lead to thrombosis, as clots are not degraded adequately.
has not yet been referenced specifically in any publications.