Analytical Data
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Gene name
IFN-gamma R1/CD119
- Application
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Alternative Names
CD119
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P15260
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Expression Region
Glu18~Gly245
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Molecular Weight
29kDa
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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
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Protein Description
Interferon-gamma receptor 1 (IFN-γ R1), also known as CD119, is a crucial component of the immune system that mediates the biological effects of interferon-gamma (IFN-γ), a cytokine integral to the immune response against infections and tumors. The binding of IFN-γ to IFN-γ R1 initiates a cascade of signaling pathways that enhances the antimicrobial activity of macrophages, promotes the differentiation of T cells, and modulates various immune functions. Dysregulation of the IFN-γ signaling pathway has been associated with several autoimmune diseases, infectious diseases, and cancers. As a result, research on IFN-γ R1 and its recombinant protein forms has gained significant interest for therapeutic purposes. Recombinant IFN-γ R1 can be utilized in experimental settings to study receptor functionality, signaling pathways, and potential interventions for diseases characterized by impaired IFN-γ responses. Moreover, the development of IFN-γ R1-based therapies could provide innovative approaches to modulate immune responses, enhancing efficacy against pathogens or tumors while minimizing autoimmune reactivity. Understanding the structure-function relationship of IFN-γ R1 and its interactions with downstream signaling molecules is essential for designing new drugs or immunotherapies targeting this receptor. Overall, the study of IFN-γ R1/CD119 recombinant protein not only enhances our knowledge of immune regulation but also offers promising avenues for clinical applications in immunotherapy and vaccine development.
