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.

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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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Interleukin-21 (IL21) is a pleiotropic cytokine produced by CD4+ T-cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation of IgG production with IL4, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL21 promotes the anti-tumorigenic activity of CD8+ T-cells and natural killer (NK) cells. IL21 exerts its effect through binding to a specific type I cytokine receptor, IL21R, which also contains the gamma chain (γc) found in other cytokine receptors, including IL2, IL4, IL7, IL9 and IL15. The IL21/IL21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.

Interleukin-21 (IL21) is a pleiotropic cytokine produced by CD4+ T-cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation of IgG production with IL4, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL21 promotes the anti-tumorigenic activity of CD8+ T-cells and natural killer (NK) cells. IL21 exerts its effect through binding to a specific type I cytokine receptor, IL21R, which also contains the gamma chain (γc) found in other cytokine receptors, including IL2, IL4, IL7, IL9 and IL15. The IL21/IL21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.