Analytical Data
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Gene name
PCI
- Application
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Alternative Names
PCI；PCI domain-containing Protein 2
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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
P05154
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Expression Region
1-406aa
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AA Sequence
MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP
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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 PCI (Plasminogen Activator Inhibitor-1) recombinant proteins has gained significant attention in recent years due to their crucial roles in various physiological and pathological processes, particularly in regulating fibrinolysis, inflammation, and cellular signaling. PCI serves as an important inhibitor of tissue plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), key enzymes in the conversion of plasminogen to plasmin, which is essential for the dissolution of blood clots. Dysregulation of PCI levels has been implicated in a range of diseases, including cardiovascular disorders, cancer, and metabolic syndromes. As a result, the development of recombinant PCI proteins has become a focal point for potential therapeutic interventions, aiming to modulate its activity for clinical benefits. Advances in recombinant DNA technology have enabled the production of these proteins with improved efficacy and stability, facilitating detailed studies on their structure-function relationships. Through this research, scientists are exploring the potential of PCI recombinant proteins as biomarkers for disease progression and as targets for novel treatment strategies. Furthermore, understanding the molecular mechanisms underlying PCI's interactions with serine proteases provides insights into the broader implications of fibrinolytic regulation and its impact on human health. The emerging findings in this field not only contribute to our understanding of coagulation and its disorders but also open avenues for innovative therapies aimed at restoring balance in the fibrinolytic system.
