This product is an active protein and may elicit a biological response in vivo, handle with caution.
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.
SDS-PAGE - Plasmin protein (Rat) (ab92813)
10% SDS-PAGE analysis of ab92813
Lane 1: ab92813 (3µg) Reduced
Lane 2: ab92813 (3µg) + Antiplasmin (10µg) Reduced
Lane 3: ab92813 (3µg) Non-reduced
Lane 4: ab92813 (3µg) + Antiplasmin (10µg) Non-reduced
Lane 5: Molecular weight markers
has not yet been referenced specifically in any publications.
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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
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