IL-1α (interleukin) is one of the three isoforms of IL-1, the other two being IL-1β and IL-1Rα. It is a proinflammatory macrophage cytokine. IL-1α is produced de novo and can either be actively secreted or can be released passively by apoptotic cells. This gene is localized to human chromosome 2q13–2q14.1.
Recombinant human IL-1α is an 18.0 kDa protein containing 159 amino acid residues.
IL-1α (interleukin) and IL-1β bind with IL-1 receptor and function as proinflammatory cytokines, whereas IL-1Rα competes to bind with IL-1R but is not proinflammatory. IL-1α can function as an intracrine molecule or as a transcription factor. IL-1 plays a major role in ischemic brain damage, as the inactivation of both IL-1α and IL-1β lead to significant suppression in brain injury. However, inactivation of only IL-1α does not have much influence on overall damage due to some compensatory modifications in the IL-1 system. A hospital-based case-control study showed th at rs3783553 variant in this gene is linked with reduced risk of breast cancer. Tumor cell production of IL-1α helps their transmigration across the endothelium, and the expression of IL-1α is linked with distant metastasis in patients with head and neck squamous cell carcinoma.
Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton.
The IL-1A is purified by proprietary chromatographic techniques.
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
