Analytical Data
-
Gene name
IFNa14
- Application
-
Alternative Names
LEIF2H; LeIF H; Interferon alpha-H; Interferon lambda-2-H
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q810G3
-
Expression Region
Cys24~Lys189
-
Molecular Weight
23kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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-14 (IFNα14) is a member of the type I interferon family, which plays a critical role in the immune response against viral infections and various diseases, including cancer. Research has shown that IFNα14 possesses unique antiviral and anticancer properties, distinguishing it from other interferon subtypes. Its mechanisms of action involve the activation of numerous pathways, leading to the enhancement of immune responses and the inhibition of viral replication. The interest in recombinant IFNα14 is driven by its potential therapeutic applications, particularly in the treatment of chronic viral infections like hepatitis C and certain types of cancers. Moreover, studies have indicated that it can modulate the tumor microenvironment, promoting anti-tumor immunity and potentially leading to better clinical outcomes in cancer therapy. Understanding the structure-function relationship of IFNα14 and optimizing its recombinant production can pave the way for novel therapeutic strategies. Furthermore, the exploration of its interactions with the immune system and its ability to trigger specific signaling pathways can provide insights into its efficacy and limitations. Overall, the development of recombinant IFNα14 is poised to make significant contributions to both virology and oncology, offering promising avenues for enhanced treatment methodologies in complex diseases.
