Native rat Plasmin protein is a Rat Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
Native
Tag free
SDS-PAGE
Yes
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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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 (By similarity).Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.
Plasminogen, Plg
Native rat Plasmin protein is a Rat Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE.
>95% SDS-PAGE
Native
Tag free
SDS-PAGE
Yes
Activity: 100% by definition (eluted from SBTI)
1 ug of plasmin corresponds to 0.024 CU or to 0.028 CTA-U.
Q01177
No
Rat
pH: 7.4
Constituents: 2.38% HEPES, 0.58% Sodium chloride
Liquid
Prepared from plasminogen by activation with immobilized Human uPA.
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 (By similarity).
Belongs to the peptidase S1 family. Plasminogen subfamily.
In the presence of the inhibitor, the activation involves only cleavage after Arg-581, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity).
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Spectrophotometric Data:
Ultraviolet: Absorbance (280nm) = 4.5
Epsilon 0.1% = 1.69
Active Concentration = 2.66 mg/mL
This supplementary information is collated from multiple sources and compiled automatically.
Plasmin a serine protease enzyme with a mass of approximately 79 kDa is an important player in the fibrinolytic system. Commonly referred to by alternate names like profibrinolysin or fibrinolysin it is mainly expressed in the liver and circulates in the blood as an inactive zymogen called plasminogen. Plasminogen is activated to plasmin through the action of activators such as tissue plasminogen activator (tPA) and urokinase (uPA). The activation to plasmin involves a cleavage at specific peptide bonds which exposes the active site that allows it to function as a protease.
The enzyme plasmin degrades fibrin in blood clots a critical function in the process of clot resolution. It belongs to the family of serine proteases and does not form part of a larger protein complex. The activity of plasmin is modulated by inhibitors like alpha-2-antiplasmin which bind to plasmin and prevent excessive degradation of fibrin. Bovine plasmin shares similar functions and serves as a model for studying human plasmin activity. Researchers often measure plasmin activity through specific assays to understand changes in fibrinolytic activity within the body.
Plasmin plays an integral role in the fibrinolytic pathway and is also involved in tissue remodeling and wound healing. The fibrinolytic pathway centers on the balance of plasminogen activation and inhibition which directly influences thrombolysis. Proteins such as tPA and uPA facilitate the conversion of plasminogen to plasmin and are tightly regulated to ensure proper physiological function. In the context of wound healing plasmin helps activate matrix metalloproteases leading to extracellular matrix breakdown and cell migration.
The regulation of plasmin is closely associated with pathological conditions such as thrombosis and liver disease. An overactive plasmin system can result in conditions like excessive bleeding or hemorrhage while inadequate plasmin activity may lead to thrombosis due to impaired clot breakdown. The interaction between plasmin and plasmin inhibitors like alpha-2-antiplasmin is critical in diseases such as liver cirrhosis where imbalances in fibrinolysis can have significant clinical outcomes. Understanding these interactions helps in developing therapeutic strategies to modulate plasmin activity in various disorders.
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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
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