| Known as | Interleukin-1 Beta; IL-1 Beta; Il1b |
|---|---|
| Derived from | E.coli |
| Purity | Greater than 95% as determined by reducing SDS-PAGE. |
| Formulation | Lyophilized from a 0.2 μm filtered solution of 50mM TrisHCl, 50mM NaCl, pH 8.0. |
| Shipping | The product is shipped at ambient temperature. |
| Storage | Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7°C for 2-7 days.Aliquots of reconstituted samples are stable at < -20°C for 3 months |
| Reconstitution | Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
| Endotoxin | Less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. |
| Background | Interleukin-1 (IL-1) designates two proteins, IL-1α and IL-1β, which are the products of distinct genes, but recognize the same cell surface receptors. IL-1α and IL-1β are structurally related polypeptides that show approximately 25% homology at the amino acid level. Both proteins are produced by a wide variety of cells in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins. The proteins are synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17.5 kDa. The specific protease responsible for the processing of IL-1β, designated interleukin 1β-converting enzyme (ICE), has been described. Mature human and mouse IL-1β share approximately 75% amino acid sequence identity and human IL-1β has been found to be active on murine cell lines. |
实验案例