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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.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

Mature human Interleukin 2 (IL2) shares 58% amino acid sequence identity with murine IL2. Human IL2 and mouse IL2 exhibit cross-species activity. 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.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

Mature mouse Interleukin 2 (IL2) shares 58% amino acid sequence identity with human IL2. It shows strain-specific heterogeneity in an N-terminal region that contains a polyglutamine stretch. Mouse and human IL2 exhibit cross-species activity. 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 independently interact 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.

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 (IL2R) consists of three subunits (55 kDa IL2RI, 75 kDa IL2RJ, 64 kDa common gamma chain Gc/IL2RG) that are present on the cell surface in varying preformed complexes. IL2/IL2R signaling is required for T-cell proliferation and other fundamental functions which are essential for an immune response. Recombinant porcine IL2 shares about 72% amino acid sequence identity with mouse, human and rat IL2. It also shares 60% and 67% acid sequence identity with rhesus macaque and Equus caballus IL2, respectively.

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.

Human interleukin-20 (IL20) is encoded by the IL20 gene located on chromosome 1, and belongs to the IL10 family that includes IL10, IL19, IL22, IL24, and IL26. IL20 is secreted by activated keratinocytes and monocytes, and signals through two distinct cell-surface receptor complexes on keratinocytes and other epithelial cells. IL20 has functions of regulating proliferation and differentiation of keratinocytes during inflammation, and causing cell expansion of multipotential hematopoietic progenitor cells. IL20 has also been used to promote tube formation of endothelial cells.

Human interleukin-21 (IL21) is encoded by the IL21 gene located on chromosome 4. IL21 is a pleiotropic cytokine produced by CD4+ T-cells in response to antigenic stimulation, and can regulate members of the immune system, like cytotoxic-T-cells or natural killer cells. Additionally, IL21 can induce division and proliferation in its target cells. IL21 elicits its effect through binding to the IL21R (IL21 receptor), which also contains the gamma chain found in other cytokine receptors such as IL2, IL4, IL7, IL9 and IL15. The IL21/IL21R interaction triggers a cascade of events, which includes the activation of the tyrosine kinases JAK1 and JAK3, which is then followed by the activation of the transcription factors STAT1 and STAT3. IL21 also seems to be an important player in clinical illnesses, including cancer immunotherapy, viral infections and allergies.

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