Analytical Data
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Gene name
IL-15R alpha & IL-15
- Application
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Alternative Names
CD_antigen: CD215
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13261
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Expression Region
31-205aa
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Molecular Weight
23.4 kDa
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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 cytokine that plays a crucial role in the immune system, particularly in the proliferation and survival of T cells and natural killer (NK) cells. IL-15 exerts its effects through a specific receptor complex, and the IL-15 receptor alpha (IL-15Rα) is a key component of this complex. Research has shown that IL-15Rα not only serves as a binding partner for IL-15 but also contributes to its trans-presentation, enhancing the cytokine's activity. The recombinant protein forms of IL-15 and IL-15Rα have garnered significant interest for their potential therapeutic applications, particularly in cancer immunotherapy and the treatment of infectious diseases. By using recombinant technologies, scientists can produce these proteins in sufficient quantities for research and potential clinical use. Studies have indicated that the combination of IL-15 with its receptor can boost the immune response, leading to improved anti-tumor activity. Furthermore, understanding the structural and functional characteristics of IL-15Rα and IL-15 is vital for designing innovative therapeutic strategies that harness the power of the immune system. This research is paving the way for novel immunotherapeutic approaches that aim to enhance immune responses in various medical conditions, illustrating the importance of IL-15 and its receptor as integral components of the immune landscape.
