Clone REA288 recognizes the precursor, secreted and membrane-associated forms of the mouse interleukin-1α (IL-1α) protein. IL-1α is a unique member in the cytokine family in the sense that the structure of its initially synthesized precursor does not contain a signal peptide fragment. After processing by the removal of N-terminal amino acids by specific proteases, the resulting peptide is called "mature" form. Both the 31kDa precursor form of IL-1α and its 18kDa mature form are biologically active. IL-1α is produced mainly by activated macrophages, as well as neutrophils, epithelial cells, and endothelial cells. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. It binds to the interleukin-1 receptor type I (IL-1R1).

Additional information: Clone REA288 displays negligible binding to Fc receptors.