Analytical Data
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Gene name
SERPINE3
- Application
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Alternative Names
SERPINE3；Serpin E3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A8MV23
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Expression Region
21-424aa
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AA Sequence
HLREGMTLLKTEFALHLYQSVAACRNETNFVISPAGVSLPLEILQFGAEGSTGQQLADALGYTVHDKRVKDFLHAVYATLPTSSQGTEMELACSLFVQVGTPLSPCFVEHVSWWANSSLEPADLSEPNSTAIQTSEGASRETAGGGPSEGPGGWPWEQVSAAFAQLVLVSTMSFQGTWRKRFSSTDTQILPFTCAYGLVLQVPMMHQTTEVNYGQFQDTAGHQVGVLELPYLGSAVSLFLVLPRDKDTPLSHIEPHLTASTIHLWTTSLRRARMDVFLPRFRIQNQFNLKSILNSWGVTDLFDPLKANLKGISGQDGFYVSEAIHKAKIEVLEEGTKASGATALLLLKRSRIPIFKADRPFIYFLREPNTGITVFFDRIQIIYQCLSSNKGSFVHYPLKNKHSF
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Molecular Weight
51.6 kDa
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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
SERPINE3, belonging to the serpin (serine protease inhibitor) superfamily, is a protein implicated in various physiological and pathophysiological processes, including inflammation, tissue remodeling, and cancer progression. Research has shown that SERPINE3 is involved in the regulation of plasminogen activators, which play a crucial role in the fibrinolytic system, impacting clot formation and resolution. Elevated levels of SERPINE3 have been associated with several diseases, such as cardiovascular disorders and certain types of cancer, indicating its potential as a biomarker for disease diagnosis and prognosis. The recombinant expression of SERPINE3 allows for detailed studies of its functional properties and interactions with other proteins, enhancing our understanding of its role in different biological contexts. This has significant implications for therapeutic applications, including the development of inhibitors or mimetics that could modulate SERPINE3 activity for clinical benefit. Given the complexity of its biological functions, ongoing research into the structure, function, and regulation of SERPINE3 is vital for harnessing its potential in disease management and treatment strategies.
