Analytical Data
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Gene name
IL2
- Application
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Alternative Names
IL2；Interleukin-2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P60568
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Expression Region
21-153aa
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AA Sequence
APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT
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Molecular Weight
41.5 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
Related Products
Protein Description
Interleukin-2 (IL-2) is a crucial cytokine in the immune system, primarily produced by T cells, and plays a significant role in regulating immune responses, including T cell growth, differentiation, and survival. The therapeutic potential of recombinant IL-2 has garnered substantial interest, particularly in the context of cancer immunotherapy and the management of autoimmune diseases. Due to its ability to enhance the proliferation of cytotoxic T lymphocytes and natural killer (NK) cells, IL-2 has been explored as a treatment option for various malignancies, such as melanoma and renal cell carcinoma. Moreover, the development of recombinant forms of IL-2 allows for specific modifications in its structure, which can improve its stability, efficacy, and safety profile. Research has also focused on optimizing dosing regimens and delivery methods to maximize clinical benefits while minimizing adverse effects. Recent advancements in biotechnological methods have facilitated the large-scale production of recombinant IL-2, making it more accessible for clinical applications. As our understanding of IL-2's mechanisms of action continues to evolve, ongoing studies aim to refine its therapeutic use, explore combination therapies, and investigate its role in personalized medicine, ultimately contributing to more effective treatments in oncology and immunology.
