IL-1β is initially synthesized as a proprotein, which is then proteolytically processed to its active form by caspase 1 (also known as interleukin 1 beta convertase) . The mature IL-1β protein is a glycosylated monomer with a molecular mass of 18-25 kDa . The glycosylation of IL-1β contributes to its stability in cell growth media and other applications .
Recombinant human IL-1β, expressed in human embryonic kidney (HEK) 293 cells, offers authentic glycosylation, which is essential for its biological activity . The production of IL-1β in HEK 293 cells ensures that the recombinant protein closely mimics the natural human protein in terms of structure and function .
IL-1β plays a pivotal role in the inflammatory response and is involved in a variety of cellular activities, including cell proliferation, differentiation, and apoptosis . It is an important mediator of the inflammatory response and is known to induce the expression of cyclooxygenase-2 (COX-2) in the central nervous system, contributing to inflammatory pain hypersensitivity .
Additionally, IL-1β, in combination with IL-23, induces the expression of IL-17, IL-21, and IL-22 by γδ T cells, suggesting its involvement in the modulation of autoimmune inflammation . Different inflammasome complexes recognize danger signals and activate the production of IL-1β and IL-18, playing a role in various diseases such as type 2 diabetes mellitus, Alzheimer’s disease, obesity, and atherosclerosis .
Recombinant human IL-1β is widely used in research and clinical applications due to its role in immune and inflammatory responses. It is suitable for cell culture and is endotoxin tested to ensure its safety and efficacy in various experimental setups . The recombinant protein is available in lyophilized form and can be reconstituted for use in various assays and studies .