Interleukins

Rat Interleukin 17A (IL17A) belongs to the IL17 family that contains IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. All of the members of the IL17 family are proinflammatory cytokines that share four conserved cysteine residues, but diverge at the N-terminus. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers, and mature IL17 contains one potential N-linked glycosylation site. IL17 is a T-cell expressed pleiotropic cytokine that regulates the activities of NF-kappaB and mitogen-activated protein kinases, and can stimulate the expression of IL-6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO).

IL17B, also named IL20, NIRF and ZCYTO7, belongs to the IL17 family and it stimulates the release of tumor necrosis factor alpha (TNF-α) and IL1-beta from the monocytic cell line THP-1. IL17B mRNA is expressed in adult pancreas, small intestine, and stomach. The IL17 family is comprised of at least six proinflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL17 family members are glycoproteins secreted as dimers that induce local cytokine production and recruit granulocytes to sites of inflammation. IL17B binds the IL17B receptor, but not the IL17 receptor; it is most homologous with IL17D, which is expressed by resting CD4+ T cells and CD19+ B cells. Immunohistochemical analysis of several nerve tissues indicates that this cytokine is primarily localized to neuronal cell bodies.

Human interleukin-17F (IL17F) is encoded by the IL17F gene located on chromosome 6, and belongs to the IL17 family, which contains: IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. IL17F shares 50% homology to the crystal structure of IL17A, and is expressed by activated T-cells. IL17 can stimulate the production of other cytokines such as IL6, IL8 and granulocyte colony-stimulating factor. IL17 also plays a role in the proliferation of PBMCs (peripheral blood mononuclear cells) and T-cells, the regulation of cartilage matrix turnover, and the inhibition of angiogenesis.

Human interleukin-19 (IL19) is encoded by the IL19 gene, which is located on chromosome 1. The protein belongs to the IL10 family of interleukins, which includes: IL10, IL20, IL22, IL24, and IL26. As a monomer made of seven amphipathic helices, IL19 has a helical bundle and shares the same cell surface receptor (IL20R) with IL20 and IL24. IL19 may play an important roles in inflammatory responses because it promotes the upregulation of IL6 and TNF-α, induces apoptosis, and activates the autoantibody production in B-cells.

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.

Interleukin-1 receptor antagonist (IL1RN) was initially called the interleukin-1 (IL1) inhibitor, which is encoded by the IL1RN gene and is a member of the IL1 cytokine family. IL1RN is secreted by various types of cells, including immune cells, epithelial cells and adipocytes. In addition, IL1RN inhibits the activity of IL1 by binding to the receptor IL1R1 and preventing its association with the co-receptor IL1RAP for signaling. IL1RN is also used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL1 plays a key role. The murine IL1RN is a single nonglycosylated polypeptide chain containing 152 amino acids and 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 IL1B and 19% homology to IL1A. It also shares 90% amino acid sequence identity with rat IL1RN.

Rat recombinant interleukin-1 receptor antagonist protein (IL1RN) was initially called the IL1 inhibitor which is encoded by the IL1RN gene. IL1RN is a member of the interleukin-1 (IL1) cytokine family, and is secreted by various types of cells including immune cells, epithelial cells and adipocytes. IL1RN can inhibit the activity of IL1 by binding to the IL1R1 receptor and preventing its association 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 rat IL1RN is a single nonglycosylated polypeptide chain, containing 152 amino acids that has been shown to block the inflammatory responses induced by IL1 both in vitro and in vivo.

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IL1RN, initially called the IL1 inhibitor, is encoded by the IL1RN gene and is a member of the interleukin 1 cytokine family. IL1RN is secreted by various types of cells including immune cells, epithelial cells, and adipocytes. ILRN functions to inhibit the activity of IL1 by binding to receptor IL1R1, preventing its association with the co-receptor IL1RAP for signaling. IL1RN is also used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL1 plays a key role. The porcine IL1RN is a single non-glycosylated polypeptide chain that has been shown to block the inflammatory responses induced by IL1 both in vitro and in vivo.

IL2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. It is expressed by CD4+ and CD8+ T-cells, γδ T-cells, B-cells, dendritic cells, and eosinophils. The receptor for IL2 consists of three subunits that are present on the cell surface in varying preformed complexes. The 55 kDa IL2 Rα is specific for IL2 and binds with low affinity. The 75 kDa IL2 Rβ, which is also a component of the IL15 receptor, binds IL2 with intermediate affinity. The 64 kDa common gamma chain γc/IL2 Rγ, which is shared with the receptors for IL4, IL7, IL9, IL15 and IL21, does not interact independently with IL2. Upon ligand binding, signal transduction is performed by both IL2 Rβ and γc. It drives resting T-cells to proliferate and induces IL2 and IL2 Rα synthesis. It contributes to T-cell homeostasis by promoting the Fas-induced death of naive CD4+ T-cells but not activated CD4+ memory lymphocytes. IL2 plays a central role in the expansion and maintenance of regulatory T-cells, although it inhibits the development of Th17 polarized cells. This recombinant IL2 has been modified by substituting a serine for cysteine at position 141 of the original sequence.