Analytical Data
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Gene name
IL-15R alpha & IL-15
- Application
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Alternative Names
IL-15 R alpha; CD215; IL-15RA; MGC104179
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Species
Rat
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
F1M293
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Expression Region
Ile10~Thr239
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Molecular Weight
60kDa
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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
Interleukin-15 (IL-15) is a crucial cytokine involved in immune responses, particularly in the development, activation, and proliferation of natural killer (NK) cells and memory CD8+ T cells. The IL-15 receptor (IL-15R) is a complex system composed of three subunits: IL-15R alpha (IL-15Rα), IL-2R beta (IL-2Rβ), and common gamma chain (γc). Among these, IL-15Rα plays a significant role in the binding and presentation of IL-15 to its receptor complex, facilitating signaling pathways that promote cell survival and proliferation. Research on recombinant forms of IL-15, particularly those fused with IL-15Rα, has garnered attention due to their potential therapeutic applications in cancer immunotherapy and the treatment of immunodeficiencies. The combination of IL-15 with its receptor alpha enhances the stability, bioavailability, and specificity of IL-15, leading to improved immune responses. Studies have shown that recombinant IL-15 and IL-15Rα fusion proteins can enhance the proliferation and function of NK cells and CD8+ T cells, making them promising candidates for clinical applications. Understanding the molecular interactions of IL-15 and IL-15Rα is essential for optimizing these recombinant proteins and developing novel immunotherapeutic strategies. This area of research is crucial for advancing our knowledge of cytokine biology and harnessing the immune system to target various malignancies and infectious diseases effectively.
