Recombinant mouse IL-1alpha (carrier-free)

IL-1 was isolated from human blood that had been exposed to a pathogenic bacterium. IL-1 is a pyrogen, and it is an activating factor for lymphocytes. It also damaged joints and influenced liver proteins (3). IL-1alpha binds to the cell surface type I and II IL-1 receptors (IL-1RI and IL-1RII). IL-1 and -beta and IL-1RA can compete for binding to these receptors. However, only IL-1RI, not IL-1RII, is functional because IL-1RII lacks a cytoplasmic domain and is thus unable to transmit signals to downstream steps (4). During ovarian inflammatory response, proinflammatory cytokine production such as IL-1 is augmented in granulosa cells and can induce local chemokine synthesis, which in turn may affect ovarian function (1). Also, IL-1 is involved in regulating tissue chemokine expression and leukocyte accumulation. The abundant influx of leukocytes into the ovary varies with the stage of the cycle and the leukocytes are thought to have a central role in influencing follicular atresia, ovulation, and luteal function and are potentially involved in ovarian disorders such as premature ovarian failure and polycystic ovary syndrome (1). IL-1a induces CXCl1 RNA and protein in mouse granulose cells.