Analytical Data
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Gene name
IL-1α
- Application
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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
SAPFSFLSNV KYNFMRIIKY EFILNDALNQ SIIRANDQYL TAAALHNLDE AVKFDMGAYK SSKDDAKITV ILRISKTQLY VTAQDEDQPV LLKEMPEIPK TITGSETNLL FFWETHGTKN YFTSVAHPNL FIATKQDYWV CLAGGPPSIT DFQILENQA
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Molecular Weight
18.0 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
Related Products
Protein Description
Interleukin-1 alpha (IL-1α) is a pro-inflammatory cytokine that plays a crucial role in the immune response, inflammation, and various physiological processes. It is primarily produced by activated macrophages and is essential for host defense mechanisms against infections and tissue injury. Research on IL-1α has gained prominence due to its involvement in a variety of pathological conditions, including autoimmune diseases, chronic inflammatory diseases, and certain types of cancer. Dysregulation of IL-1α production and signaling can lead to excessive inflammation and tissue damage, making it a target for therapeutic intervention. The recombinant form of IL-1α has been developed for use in both basic research and potential clinical applications. In laboratory settings, recombinant IL-1α is utilized to study its biological effects on immune cells, its role in inflammatory responses, and its implications in disease models. Furthermore, understanding the functional mechanisms of IL-1α can aid in the development of novel therapies, including IL-1 receptor antagonists, which are currently employed to treat various inflammatory disorders. Overall, the study of IL-1α recombinant protein is vital for advancing our knowledge of immune regulation and for identifying new avenues for therapeutic intervention in inflammation-related diseases.
