Recombinant Human Interleukin-1 beta

Recombinant Human Interleukin-1 beta (rhIL-1b) is a secreted pro-inflammatory cytokine belonging to the IL-1 family, produced primarily by activated monocytes, macrophages, and dendritic cells. The human IL-1b precursor (pro-IL-1b, 269 amino acids) is synthesized as an inactive cytoplasmic protein that undergoes proteolytic cleavage by caspase-1 (IL-1b-converting enzyme) to yield the mature 17 kDa cytokine. IL-1beta binds to the Interleukin-1 receptor type I (IL-1RI), triggering MyD88-dependent NF-kappaB and MAPK signaling cascades that promote expression of inflammatory mediators, cell adhesion molecules, and acute-phase proteins. IL-1beta plays a central role in mediating innate and adaptive immune responses, fever induction, leukocyte recruitment, and tissue remodeling. Dysregulated IL-1beta activity is implicated in numerous inflammatory and autoimmune disorders, including rheumatoid arthritis, gout, type 2 diabetes, and atherosclerosis. Recombinant Human IL-1beta corresponds to the mature form of the cytokine with an additional N-terminal His tag for bacterial expression, yielding a total length of 171 amino acids. The protein is biologically active and retains full receptor-binding and signaling properties