Analytical Data
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Gene name
SerpinA5
- Application
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Alternative Names
SERPINA5;PCI;PLANH3;PROCI;Plasma serine protease inhibitor
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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
20-406aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMHRHHPREMKKRVEDLHVGATVAPSSRRDF TFDLYRALASAAPSQNIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLN LQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSA MKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVI MVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDR NLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQ LELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMV HKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNIL FLGKVNRP
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Molecular Weight
46 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
SerpinA5, also known as Protein C Inhibitor (PCI), is a member of the serine protease inhibitor (serpin) superfamily, playing a crucial role in regulating coagulation and inflammation. Its primary function is to inhibit activated protein C (APC), a key player in the coagulation cascade, thereby preventing excessive bleeding during vascular injury. Increased levels of SerpinA5 have been linked to various pathological conditions, including thrombosis, inflammatory diseases, and cancer progression. Research has expanded to explore its dual role in both thrombosis and cancer, where it may influence tumor growth and metastatic potential. Recombinant SerpinA5 has gained attention for its potential therapeutic applications, including its use in the development of anticoagulant therapies and as a biomarker for disease prognosis. Understanding the structure-function relationship of SerpinA5 through recombinant protein studies could unveil novel approaches to modulate its activity, offering insights into the design of inhibitors or mimetics that could be beneficial in clinical settings. Furthermore, these studies provide valuable information on the molecular mechanisms underlying its interactions with proteases, paving the way for enhanced therapeutic strategies in managing diseases associated with dysregulated coagulation and inflammation. Thus, the research on recombinant SerpinA5 is pivotal for both basic biology and potential clinical applications.
