Analytical Data
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Gene name
PLAU/uPA
- Application
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Alternative Names
PLAU; ATF; URK; UK; UP-A; Abbokinase; Urokinase-Type Plasminogen Activator
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P06869
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Expression Region
Ile180~Phe433
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Molecular Weight
32kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of PLAU (plasminogen activator, urokinase) and its recombinant protein, uPA (urokinase-type plasminogen activator), is significant in the field of biochemistry and medical research due to its crucial role in fibrinolysis and tissue remodeling. UPA is a serine protease that converts plasminogen into plasmin, initiating the degradation of fibrin in blood clots, which is vital for normal hemostasis and wound healing. Dysregulation of uPA is implicated in various pathological conditions, including cancer metastasis, where increased uPA activity is associated with tumor invasion and poor prognosis. Research into the recombinant expression of uPA has enabled the production of this protein for therapeutic and diagnostic applications. Recombinant uPA can be utilized in targeted therapies for thrombotic disorders, as well as in understanding its mechanisms in cancer progression. The ability to produce uPA in a controlled manner through recombinant techniques enhances the potential for developing novel treatments and improving patient outcomes. Furthermore, studies assessing the interactions of uPA with other proteins in the plasminogen activation system continue to provide insights into its biological functions and therapeutic potential, making it a focal point of ongoing research in both vascular biology and oncology.
