Analytical Data
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Gene name
IFNa
- Application
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Alternative Names
IFNa；Interferon alpha-8
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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
P01562
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Expression Region
24-189aa
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AA Sequence
M+CDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE
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Molecular Weight
19.5 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
Interferon alpha (IFNα) is a type of cytokine with significant roles in the immune response against viral infections, as well as in modulating various cellular processes. Given its important therapeutic potential, especially in treating viral hepatitis, certain types of cancer, and autoimmune diseases, research into recombinant IFNα production has gained traction. Scientists have explored various expression systems, including bacterial, yeast, and mammalian cells, to produce biologically active forms of IFNα more efficiently and at a lower cost. Advances in genetic engineering and protein purification techniques have further enhanced the yield and quality of recombinant IFNα. Additionally, the understanding of its mechanism of action on immune cells, alongside the identification of specific receptor interactions, has paved the way for targeted therapies and combinatorial treatments. The research is not only focused on expanding the therapeutic applications of IFNα but also on overcoming challenges such as potential side effects and resistance mechanisms. Consequently, the study of recombinant IFNα continues to be a dynamic field, merging basic research with clinical applications to improve the outcome for patients suffering from various diseases influenced by viral infections and immune dysregulation.
