Description
Key facts
Purity:>95% SDS-PAGE,
Expression system:Native,
Tags:Tag free,
Applications:SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:15 units/mg proteinOne unit is defined as the amount of enzyme that hydrolyzes one μmole of tosyl-Gly-Pro-Lys-pNA per minute at 25°C, pH 7.8. Note: One unit = 1.25 CU.,
Accession:P00747,
Animal free:No,
Carrier free:No,
Species:Human,
Reconstitution:Reconstitute in water,
Storage buffer:pH: 7.4Constituents: 0.946% D-(+)-Trehalose dihydrate, 0.24% Sodium dihydrogen phosphate
Product details:
The Native human Plasmin protein (Active) ab90928 is prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
Ensure the validity of your result using our native human Plasmin protein as a positive control in SDS-PAGE. The bioactive native human Plasmin ab90928 has been prepared by using streptokinase to activate human plasma plasminogen.
Check out our protein gel staining guide for SDS-PAGE
Protein Determination: Extinction Coefficient (ε) 0.1% at 280 nm 1cm pathway = 1.71
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C
Supplementary Information:
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.
Biological function summary
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.
Pathways
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.
