Analytical Data
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Gene name
IRF9
- Application
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Alternative Names
ISGF3G; hIRF9
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Species
Human
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00978
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Expression Region
M1-V393
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Protein Length
Full Length
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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 regulatory factor 9 (IRF9) is a critical transcription factor involved in the immune response, particularly in mediating the effects of type I interferons (IFNs). Research on IRF9 has gained prominence due to its essential role in various biological processes, including the antiviral response, immune regulation, and oncogenesis. This protein forms a complex with other STAT proteins, particularly STAT1 and STAT2, to promote the transcription of interferon-stimulated genes (ISGs), which are pivotal in enhancing the host's defense against viral infections. The dysregulation of IRF9 has been implicated in various pathological conditions, such as autoimmune diseases and cancer, making it a promising target for therapeutic interventions. Recent studies have focused on the characterization and production of recombinant IRF9 protein to better understand its structure-function relationships and regulatory mechanisms. The availability of recombinant IRF9 can facilitate high-throughput assays and functional studies aimed at exploring its interactions with other signaling pathways, assessing its role in immune modulation, and evaluating its potential as a biomarker or target for drug development. Given the increasing need for effective antiviral therapies and the complex nature of immune responses, the exploration of IRF9 and its therapeutic implications continues to be an exciting area of research in molecular and cellular biology.
