Analytical Data
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Gene name
IL2RB-IL2RA-IL2RG
- Application
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Alternative Names
High affinity IL-2 receptor subunit betap70-75; CD122
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Species
Mouse
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16297
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Expression Region
24-240aa
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Molecular Weight
29.3 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
The study of the IL2RB-IL2RA-IL2RG recombinant protein focuses on the crucial roles of interleukin-2 (IL-2) signaling in immune regulation and homeostasis. IL-2 is a key cytokine involved in the proliferation and differentiation of T cells, which are essential for adaptive immunity. The interaction between IL-2 and its receptors, composed of the IL-2 receptor beta (IL2RB), IL-2 receptor alpha (IL2RA), and IL-2 receptor gamma (IL2RG), is vital for mediating IL-2's effects on immune cells. Disruptions in this signaling pathway can lead to various immunological disorders, including autoimmune diseases and cancers. Recent advances in recombinant DNA technology have enabled the production of IL2RB-IL2RA-IL2RG fusion proteins, allowing for more detailed studies of their structure, function, and potential therapeutic applications. These recombinant proteins can serve as valuable tools for investigating the molecular mechanisms underlying IL-2 signaling, as well as for developing new immunotherapies aimed at enhancing or modulating immune responses. By understanding the intricacies of IL-2 receptor interactions through recombinant protein studies, researchers aim to provide insights that could lead to innovative treatments for diseases characterized by dysregulated immune responses.
