Human IL-1 alpha/IL-1A Protein
Catalog No: IL1A-HP001
- Species
- Human
- Expression System
- E. coli
- Activity
- Activity verified
Product overview
Recombinant Human IL-1 alpha/IL-1A Protein is expressed in E. coli without tag. It contains amino acid residues Ser113-Ala271 (accession: NP_000566.3).
Product Details
- Molecular Aliases
- Interleukin-1 alpha; IL-1 alpha; Hematopoietin-1; IL1A; IL1F1; IL-1 ALPHA; IL1α; IL-1A; IL1
- Protein Length
- Ser113-Ala271
- Expression System
- E. coli
- Theoretical Molecular Weight
- The protein has a predicted MW of 18 kDa same as Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
- Endotoxin
- Less than 0.05 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display

Human IL-1 alpha on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.

The purity of Human IL-1 alpha is greater than 95% as determined by SEC-HPLC.

Measured by a reporter gene assay. The ED50 for this effect is 1-15 pg/mL. (QC Test)

Human IL-1R1, His Tag (Cat. IL1-HM1R1) captured on CM5 Chip via anti-his antibody can bind Human IL-1 alpha, No tag with an affinity constant of 0.51 nM as determined in SPR assay (Biacore T200). (QC Test)

Loaded Human IL-1R1, His Tag (Cat. IL1-HM1R1) on Anti-His-Biosensor can bind Human IL-1 alpha, No Tag with an affinity constant of 0.84 nM as determined in BLI assay.
Background
The interleukin (IL)-1 family of cytokines is currently comprised of 11 members that have pleiotropic functions in inflammation and cancer. IL-1α and IL-1β were the first members of the IL-1 family to be described, and both signal via the same receptor, IL-1R. Over the last decade, much progress has been made in our understanding of biogenesis of IL-1β and its functions in human diseases.
References
- Malik A, Kanneganti TD. Function and regulation of IL-1α in inflammatory diseases and cancer. Immunol Rev. 2018 Jan;281(1):124-137. doi: 10.1111/imr.12615. PMID: 29247991; PMCID: PMC5739076.
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