IL-1 alpha Protein, Mouse (HEK293, His)

The cytokine interleukin-1 alpha (IL-1 alpha), present constitutively intracellularly in almost all quiescent non-hematopoietic cells, serves a crucial role in inflammation and acts as a bridge between the innate and adaptive immune systems. Upon binding to its receptor IL1R1, in conjunction with its accessory protein IL1RAP, it forms the high-affinity interleukin-1 receptor complex. Subsequent signaling events involve the recruitment of adapter molecules such as MYD88, IRAK1, or IRAK4, leading to the activation of NF-kappa-B and the three MAPK pathways—p38, p42/p44, and JNK pathways. Intracellularly, IL-1 alpha functions as an alarmin, and upon cell death, it is released into the extracellular space following cell membrane disruption, inducing inflammation and signaling host response to injury or damage. Beyond its role as a danger signal released during cell necrosis, IL-1 alpha also directly senses DNA damage, serving as a signal for genotoxic stress without compromising cell integrity. Additionally, IL-1 alpha interacts with various proteins, including TMED10, facilitating translocation from the cytoplasm into the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) and subsequent secretion. Its interaction with IL1R1 and S100A13 further contributes to its intricate regulatory mechanisms, with the latter being a crucial step in the export of IL-1 alpha, involving direct translocation of the complex across the plasma membrane.