Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological, hematopoietic activities, and plays one of the central roles in the regulation of the immune responses. Both IL1A and IL-1B bind to the same receptor and have similar biological properties. Among various species, the amino acid sequence of mature IL1A is conserved 60% to 70% and human IL1A has been found to be biologically active with murine cell lines.

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Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar biological properties. These cytokines have a broad range of activities including stimulation of thymocyte proliferation by inducing IL2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1B is a secreted cytokine, IL1A is predominantly a cell associated cytokine.

Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological and hematopoietic activities, and plays one of the central roles in the regulation of immune responses. Both IL1A and IL1B bind to the same receptor and have similar but not identical biological properties. Recombinant rat IL1A contains 150 amino acids, which is a single nonglycosylated polypeptide.

Interleukin 1 alpha (IL1α) is a non-secreted proinflammatory cytokine 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. Both IL1α and IL1β binds to the same receptor and has similar if not identical biological properties. Recombinant rhesus macaque IL1 alpha contains 150 amino acids which is a single nonglycosylated polypeptide. Among various species, the amino acid sequence of mature IL1α is conserved 60% to 70% and human IL1 has been found to be biologically active on murine cell lines.

Interleukin-1 beta (IL1B) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological and hematopoietic activities, and plays one of the central roles in the regulation of immune responses. Both IL1A and IL1B bind to the same receptor and have similar but not identical biological properties.

Interleukin-1 beta (IL1B) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological, hematopoietic activities, and plays one of the central roles in the regulation of the immune responses. Both IL1A and IL1B bind to the same receptor and have similar but not identical biological properties.

Interleukin-1 beta (IL1B) is a pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities, including the stimulation of thymocyte proliferation, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1A is predominantly a cell associated cytokine, IL1B is a secreted cytokine.

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Interleukin-1 beta (IL1B) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological and hematopoietic activities, and plays one of the central roles in the regulation of immune responses. Both IL1A and IL1B bind to the same receptor and have similar biological properties. Recombinant porcine IL1B shares 63-70% amino acid sequence identity with canine, cotton rat, equine, feline, human, mouse, rat and rhesus IL1B.

Interleukin-1 beta (IL1B) is a pro-inflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar biological properties. These cytokines have a broad range of activities, including stimulation of thymocyte proliferation, by inducing IL2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1A is predominantly a cell associated cytokine, IL1B is a secreted cytokine.

IL1B is a pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including, stimulation of thymocyte proliferation by inducing IL2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1A is predominantly a cell associated cytokine, IL1B is a secreted cytokine. The 17.3 kDa mature rhesus IL1B shares 98% amino acid sequence identity with human IL-1B.

IL1RN, initially called the IL1 inhibitor, is encoded by the IL1RN gene which is a member of the interleukin 1 cytokine family. IL1RN is secreted by various types of cells, including immune cells, epithelial cells and adipocytes. IL1RN functions to inhibit the activity of interleukin-1 by binding to the IL1R1 receptor, which prevents it from associating with the co-receptor IL1RAP. IL1RN is also used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL1 plays a key role. The Equus caballus IL1RN is a single nonglycosylated polypeptide chain that has been shown to block the inflammatory responses induced by IL1 both in vitro and in vivo. The protein shows 26% amino acid homology to IL1β and 19% homology to IL1α.

Interleukin-1 receptor antagonist (IL1RN) is a member of the IL1 family. IL1RN is secreted by various types of cells including immune cells, epithelial cells and adipocytes, and is a natural inhibitor of the pro-inflammatory effect of IL1B. This protein also inhibits the activities of IL1A and modulates a variety of interleukin 1 related immune and inflammatory responses. IL4 and IL13 have been shown to amplify the stimulatory effect of IL1B on the production of soluble and intracellular forms of IL1RN. The regulated expression of IL1RN in various cell types has been shown to be influenced by cytokines. In synovial fibroblasts the synthesis of IL1RN is markedly enhanced by IL1, TNF-α, or PDGF. The protein shows 26% amino acid homology to IL1B and 19% homology to IL1A.