Description : |
Interleukin-1 (IL-1) is a family of cytokines that play a central role in the regulation of immune and inflammatory responses to infections or sterile insults. IL-1α and IL-1β are the first two members discovered in this family, which are the products of distinct genes recognizing 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 is interleukin 1β-converting enzyme (ICE)/caspase-1. Mature human and mouse IL-1β share approximately 75% amino acid sequence identity where human IL-1β has been found to be active on murine cell lines. |
Source : |
CHO Cells |
Species : |
Mouse |
Form : |
Lyophilized after extensive dialysis against PBS. |
Bio-activity : |
ED50< 10 pg/ml, measured in a cell proliferation assay using d10s cells, corresponding to a specific activity of>1×108 units/mg. |
Molecular Mass : |
17.4 kDa, observed by non-reducing SDS-PAGE. |
AA Sequence : |
Val118-Ser269. |
Endotoxin : |
<0.2 eu/μg, determined by lal>0.2> |
Purity : |
>95% as analyzed by SDS-PAGE and HPLC. |
Storage : |
Lyophilized recombinant protein remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rmIL-1beta should be stable up to 1 week at 4°C or up to 2 months at -20°C. |
Reconstitution : |
Reconstituted in ddH2O or PBS at 100 μg/ml. |