Analytical Data
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Gene name
Il1a
- Application
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Alternative Names
IL1A;IL1F1;Interleukin-1 alpha
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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
P01583
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Expression Region
113-271aa
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AA Sequence
SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA
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Molecular Weight
20.0 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-1 alpha (IL-1α) is a key cytokine in the immune response, playing a crucial role in the regulation of inflammation and the activation of immune cells. It is primarily produced by activated macrophages and epithelial cells, and is involved in a wide array of biological processes, including cellular proliferation, differentiation, and apoptosis. The dysregulation of IL-1α is linked to various inflammatory diseases, autoimmune disorders, and even cancer, making it a significant target for therapeutic interventions. Research on recombinant IL-1α has gained momentum due to its potential applications in understanding these diseases and developing novel treatments. By producing recombinant IL-1α, scientists aim to explore its functional properties, investigate its signaling pathways, and evaluate its effects on various cell types in vitro and in vivo. Furthermore, recombinant IL-1α can be utilized in drug development, vaccine formulation, and therapeutic strategies for managing diseases associated with aberrant IL-1 signaling. The growing interest in targeted therapies has fueled studies on its structure-function relationship and the development of IL-1α inhibitors, indicating its promise in improving clinical outcomes for patients suffering from IL-1-related pathologies. Overall, the research on recombinant IL-1α continues to advance our understanding of its crucial role in immune modulation and highlights its relevance in developing effective therapeutic strategies for diverse diseases.
