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Recombinant Human Interleukin-1 alpha produced in E.coli is a single non-glycosylated polypeptide chain containing 159 amino acids and having a molecular mass of approximately 18 KDa.
Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of murine D10S cells is less then 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.
Less than 1EU/mg of rHuIL-1α as determined by LAL method.
>97% by SDS-PAGE and HPLC analyses.
This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
Crystal structure of IL-1a (PDB2ILA).
IL-1 alpha is a non-secreted proinflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL-1alpha and IL-1beta binds to the same receptor and has similar if not identical biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation, by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1beta is a secreted cytokine, IL-1alpha is predominantly a cell-associated cytokine.
interleukin-1 receptor binding, protein binding, signal transducer activity.