Human IL-1 alpha/IL-1F1 Biotinylated Antibody

IL-1 alpha and IL-1 beta are both synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17,000 Da. Neither precursor contains a typical hydrophobic signal peptide sequence and most of the precursor form of IL-1 alpha remains in the cytosol of cells, although there is evidence for a membrane-bound form of the precursor form of IL-1 alpha. The IL-1 alpha precursor reportedly shows full biological activity in the EL-4 assay. Among various species, the amino acid sequence of mature IL-1 alpha is conserved 60% to 70% and human IL-1 has been found to be biologically active on murine cell lines. Both forms of IL-1 bind to the same receptors, designated type I and type II. Evidence suggests that only the type I receptor is capable of signal transduction and that the type II receptor may function as a decoy, binding IL-1 and thus preventing binding of IL-1 to the type I receptor.