Interleukins

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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.

IL22 is part of the IL10 family of regulatory cytokines, which includes IL10, IL19, IL20, IL22, IL24 and IL26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by activated T-lymphocytes and dendritic cells, IL10 contributes to the inflammatory response in vivo. IL22 uses CRF2-4, a member of the class II cytokine receptor family, and IL22R, IL22 receptor, to produce its downstream effects. IL22 and IL17 are rapidly produced by splenic lymphoid tissue inducer–like cells (LTi-like cells) and Th17 cells and likely plays a role in the coordinated response of both the adaptive and innate immune systems.

IL22 belongs to the IL10 family of regulatory cytokines, which includes IL10, IL19, IL20, IL22, IL24 and IL26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T-lymphocytes and dendritic cells, IL10 contributes to the inflammatory response in vivo. IL22 signals through CRF2-4 and IL22. IL22 along with IL17 are rapidly produced by splenic lymphoid tissue inducer–like cells (LTi-like cells) and can be also produced by Th17 cells. It is also likely that IL22 plays a role in the coordinated response of both the adaptive and innate immune systems. Recombinant mouse interleukin-22 contains 147 amino acids and has approximately 81% and 92% amino acid sequence identity with human and rat IL22, respectively.

IL22 belongs to IL10 family of regulatory cytokines, which includes IL10, IL19, IL20, IL22, IL24 and IL26. Members of this family share partial homology in their amino acid sequences, but are dissimilar in their biological functions. Produced by T-lymphocytes and dendritic cells, IL10 contributes to the inflammatory response in vivo, and signals through CRF2-4 and IL22. Along with IL17, it is rapidly produced by splenic LTi-like cells and can be also produced by Th17 cells. It is likely that IL22 plays a role in the coordinated response of both the adaptive and innate immune systems.

Interleukin-3 beta (IL3B) and IL3A are two variants of IL3. IL3A and IL3B are identical aside from the fact that IL3A has three extra amino acids inserted at position 56. IL3 is a hematopoietic growth factor that promotes the survival, differentiation and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil and mast cell lineages. Produced by T-cells, mast cells and eosinophils, IL3 enhances thrombopoieses, phagocytosis and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL3 may have additional immunoregulatory roles. Many of the IL3 activities depend upon co-stimulation with other cytokines. IL3 is a species-specific, variably glycosylated cytokine.

Interleukin-3 (IL3) is a hematopoietic growth factor that promotes the survival, differentiation and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil and mast cell lineages. Produced by T-cells, mast cells and eosinophils, IL3 enhances thrombopoieses, phagocytosis and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL3 may have additional immunoregulatory roles. Many of the IL3 activities depend upon co-stimulation with other cytokines. IL3 is species-specific, variably glycosylated cytokine.

Interleukin 3 is a pleiotropic factor produced primarily by activated T-cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. In addition, IL3 also affects the functional activity of mature mast cells, basophils, eosinophils and macrophages. Because of its multiple functions and targets, it was originally studied under different names, including mast cell growth factor, P-cell stimulating factor, burst promoting activity, multicolony stimulating factor, thy-1 inducing factor and WEHI-3 growth factor.

In addition to activated T-cells, other cell types can also produce IL3, such as human thymic epithelial cells, activated murine mast cells, murine keratinocytes and neurons/astrocytes. At the amino acid sequence level, mature human and murine IL3 share only 29% sequence identity. Consistent with this lack of homology, IL3 activity is highly species-specific and human IL3 does not show activity on murine cells.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. In addition, IL3 also affects the functional activity of mature mast cells, basophils, eosinophils and macrophages. Because of its multiple functions and targets, it was originally studied under different names, including mast cell growth factor, P-cell stimulating factor, burst promoting activity, multicolony stimulating factor, thy-1 inducing factor and WEHI-3 growth factor.

In addition to activated T cells, other cell types can also produce IL3, such as human thymic epithelial cells, activated murine mast cells, murine keratinocytes and neurons/astrocytes. At the amino acid sequence level, mature human and murine IL3 share only 29% sequence identity. Consistent with this lack of homology, IL3 activity is highly species-specific and human IL3 does not show activity on murine cells.

Interleukin-3 (IL3) is an interleukin which is a type of biological signal (cytokine) encoded by the IL3 gene located on chromosome 5, and produced primarily by activated T-cells, human thymic epithelial cells, activated murine mast cells, murine keratinocytes and murine neurons/astrocytes. The protein acts in hematopoiesis by controlling the production, differentiation and function of two related white cell populations in the blood: the granulocytes and the monocytes/macrophages. The rhesus macaque IL3 reported to be a monomer, as it is known, contains 124 amino acid residues, which make up a single nonglycosylated polypeptide. However, recombinant rhesus macaque, human and murine IL3 share low homology.

The human interleukin-31 (IL31) gene is located on chromosome 12, and is regulated so that IL31 is expressed in low levels in type 2 helper T-cells, which exist in the testis, bone marrow, skeletal muscle, kidney, colon, thymus, small intestine and trachea. IL31 shares several structural and functional characteristics with IL6, oncostatin M, leukemia inhibitory factor (LIF), and cardiotrophin-1. IL31 signals through the IL31 receptor A and oncostatin M receptor subunits. IL31 can also activate STAT3 through receptors and may be involved in skin immunity. Its use of regulating immune responses have been implicated in skin physiology and inflammatory skin diseases. IL31 may play a role in allergic diseases or disorders such as bronchial inflammation and asthma. Human IL31 shares 24% amino acid sequence homology with the mature mouse IL31.

IL33, encoded by the IL33 gene located on chromosome 9 in humans, is a pro-inflammatory protein belonging to the IL1 superfamily, but shares less than 20% amino acid sequence identity with other members. The mature IL33 protein has a 52-58% amino acid sequence identity with mouse and rat IL33. IL33 is secreted at high levels by high endothelial venules, which can be found in the tonsils, Peyer's patches and mesenteric lymph nodes, but not in the placenta. IL33 is upregulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL1G or IL1H stimulation. IL33 elicits its biological effects by interacting with IL1RL1/ST2, which in turn recruits MYD88, IRAK1, IRAK4, and TRAF6. This is then followed by the phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8.

Interleukin-33 (IL33) is a pro-inflammatory protein that shares structural and functional characteristics with the IL1 cytokine family. It binds and signals through the IL1RL1/ST2 receptor, activating NF-κB and MAP kinases. IL33 induces production of T-helper-2 (Th2) cell related cytokines, including IL4, IL5 and IL13, and exerts multiple inflammation-related bioactivities. It has also been reported that after addition of IL33, the levels of interferon gamma (IFNG) were reduced in polarized mouse Th1 cells.

Interleukin-33 (IL33), also known as NF-HEV and DVS 27, is a cytokine belonging to the IL1 superfamily. IL33 is a pro-inflammatory protein that may regulate gene transcription and induce helper T-cells, mast cells, eosinophils and basophils to produce type 2 cytokines. The induction of type 2 cytokines by IL33 in vivo is believed to induce the severe pathological changes observed in mucosal organs following administration of IL33. IL33 is constitutively expressed in smooth muscle and airway epithelia, and it binds to a high-affinity receptor family member ST2. In vivo administration of mature IL33 promotes increased production of IL5, IL13, IgE and IgA, as well as splenomegaly and inflammatory infiltration of mucosal tissues.