Analytical Data
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Gene name
uPA
- Application
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Alternative Names
PLAU; ATF; URK; UK; UP-A; Abbokinase; Urokinase-Type Plasminogen Activator
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Species
Pig
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P04185
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Expression Region
Ser21~Pro168
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Molecular Weight
36kDa
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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
Urokinase-type plasminogen activator (uPA) is a serine protease that plays a crucial role in the fibrinolytic system, converting plasminogen to plasmin and thereby facilitating extracellular matrix remodeling and cell migration. Its involvement in physiological processes such as tissue repair, wound healing, and cell migration has led to significant interest in its function and regulation. Moreover, uPA is implicated in various pathological conditions, particularly in cancer progression, where elevated levels of uPA are associated with increased tumor invasion and metastasis. This has made uPA a potential biomarker for cancer prognosis and a target for therapeutic intervention. The recombinant production of uPA has been pursued to study its structure-function relationships and to explore its therapeutic applications. Advances in recombinant DNA technology have enabled the generation of uPA variants with altered properties, providing insights into its enzymatic mechanisms and regulatory pathways. Research on uPA also encompasses its role in non-cancerous disorders, including cardiovascular diseases and inflammatory responses, highlighting its significance beyond oncology. As such, the ongoing investigation into uPA recombinant proteins is vital for understanding the intricate balance of its biological activities and developing strategies to modulate its function for therapeutic benefit.
