Analytical Data
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Gene name
IFNw
- Application
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Alternative Names
IFN-w; IFNo; Interferon alpha-II-1
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Species
Human
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Source
HEK293
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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
P05000
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Expression Region
Leu22~Ser195
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Protein Length
Partial
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Molecular Weight
25kDa
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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 lambda (IFNλ), a member of the type III interferon family, has garnered significant attention in recent years due to its role in the immune response against viral infections and its potential therapeutic applications. Unlike the more widely studied type I interferons (such as IFNα and IFNβ), which can have broad effects and significant side effects, IFNλ demonstrates a more targeted antiviral response, primarily affecting epithelial cells and showing limited systemic effects. This specificity could lead to a more favorable safety profile in clinical uses. Researchers have been investigating the recombinant production of IFNλ to better understand its biological functions and mechanisms. Advances in genetic engineering and protein expression technologies have facilitated the development of high-yield production systems, enabling scientists to produce large quantities of functional IFNλ for both research and therapeutic purposes. Studies have revealed its potential efficacy in treating viral infections such as hepatitis C and more recently, COVID-19, as well as its immunomodulatory effects in autoimmune conditions. Given its unique properties, ongoing research aims to elucidate the precise signaling pathways activated by IFNλ and to explore the full spectrum of its therapeutic possibilities. Understanding IFNλ's mechanisms of action could pave the way for improved treatment strategies for various viral diseases and enhance our knowledge of the immune system's responses.
