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.

Interleukin-36A (IL36A) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. Studies have shown that IL36A is mainly found in the skin and lymphoid tissues, as well as fetal brain, trachea, stomach and intestine. Notably, IL36A is the only novel IL1 family member expressed on T-cells. IL36A contains 153 amino acid residues, which make up a single nonglycosylated polypeptide that shares 57-68% amino acid sequence identity with mouse, rabbit, equine and bovine IL36A, and 27-57% amino acid sequence identity with other novel IL1 family members.

Interleukin-36A (IL36A) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. Studies have shown that IL36A is mainly found in the skin and lymphoid tissues, as well as fetal brain, trachea, stomach and intestine. Notably, IL36A is the only novel IL1 family member expressed on T-cells. IL36A contains 158 amino acid residues which make up a single nonglycosylated polypeptide that is 30% homologous in amino acid sequence to IL1ra, and 27%, 31%, 36%, 46%, 57% and 28% homologous to IL1G, IL36Ra/IL1F5, IL37/IL1F7, IL36G/IL1F8, IL36H/IL1F9 and IL1F10 respectively.

Interleukin-36A (IL36A) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B, and IL36G (formerly IL1F6, IL1F8, and IL1F9) are all IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36A is mainly found in skin and lymphoid tissues, but can also be found in fetal brain, trachea, stomach and intestine. IL36A is expressed by monocytes, B-cells and T-cells. Notably, IL36A is the only novel IL1 family member expressed on T-cells. Recombinant murine IL36A contains 153 amino acid residues, which compose a single nonglycosylated polypeptide. Specifically, mouse IL36A shares 83% amino acid sequence identity with rat IL36A, 54-60% with human, rabbit, equine and bovine IL36A.