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Recombinant Mouse IL-1 alpha produced in E. coli is a non-glycosylated polypeptide chain containing 156 amino acids and having a molecular mass of 18000 Dalton.
The ED50 as determined by the dose-dependant stimulation of mouse D10S cells was found to be less than 0.01 ng/ml, corresponding to a Specific Activity of 1.0 x 108IU/mg.
Less than 0.1ng/ug (1 IEU/ug) of IL-1α.
>98% as determined by RP-HPLC, FPLC and SDS-PAGE.
Lyophilized rmIL-1α although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rmIL-1α should be stored at 4°C between 2-7 days and for future use below -18°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Aliquot to avoid repeated freeze-thaw cycles.
It is recommended to reconstitute the lyophilized rmIL-1α in sterile 18MΩ-cm H2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.
Crystal structure of IL-1a (PDB2ILA).
IL-1α is distinct from the other agonist member of the IL-1 family, IL-1β. Although IL-1α triggers the same IL-1 receptor and although many of the biological effects of IL-1α are similar to those of IL-1α, in humans IL-1α is predominantly an intracellular molecule. In fact, there is evidence that IL-1α has both intracellular functions as a precursor molecule due to a nuclear localization sequence. IL-1α as an unprocessed precursor is biologically as active as the processed form. IL-1α is also found constitutively in epithelial cells, whereas constitutive expression of IL-1β is rare. In many ways, IL-1α appears to be closer to the fibroblast growth factor family than the secreted IL-1β form. Therapeutic stratiegies for blocking IL-1β predominate over those for blocking IL-1α. Many humans have circulating neutralizing antibodies to IL-1α but not IL-1β.