Interleukin-4 (IL4) is a pleiotropic cytokine mainly produced by mast cells, activated T-cells and bone marrow stromal cells. It has many biological roles, including the stimulation of activated B-cell and T-cell proliferation, and the differentiation of CD4+ T-cells into Th2 cells. Additionally, IL4 enhances both the secretion and expression of cell surface IgE and IgG1. IL4 also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. The rhesus macaque IL4 shares about 40-45% amino acid sequence identity with human, mouse, and rat IL4 and is species-specific in its activities.

The IL5 gene is located on chromosome 5 in humans, in close proximity to the genes encoding IL3, IL4, and granulocyte-macrophage colony-stimulating factor (CSF2), which are often co-expressed in TH2 cells. Through binding to the IL5 receptor, IL5 stimulates B cell growth and increases immunoglobulin secretion and is also a key mediator in eosinophil activation. Interleukin 5 has long been associated with the cause of several allergic diseases including allergic rhinitis and asthma. Human IL5 is 115 amino acids long (murine IL5 has 133 amino acids) and is a TH2 cytokine that is part of the hematopoietic family. Unlike other members of this cytokine family (namely IL3 and CSF2), this glycoprotein is a homodimer in its active form.

The IL5 gene is located on chromosome 11 in mice, in close proximity to the genes encoding IL3, IL4, and granulocyte-macrophage colony-stimulating factor (CSF2), which are often co-expressed in TH2 cells. Through binding to the IL5 receptor, IL5 stimulates B cell growth and increases immunoglobulin secretion and is also a key mediator in eosinophil activation. Interleukin 5 has long been associated with the cause of several allergic diseases including allergic rhinitis and asthma. Murine IL5 is a TH2 cytokine that is part of the hematopoietic family. Unlike other members of this cytokine family (namely IL3 and CSF2), this glycoprotein is a homodimer in its active form.

The IL5 gene is located on chromosome 11 in rats, in close proximity to the genes encoding IL3, IL4, and granulocyte-macrophage colony-stimulating factor (CSF2), which are often co-expressed in TH2 cells. Through binding to the IL5 receptor, IL5 stimulates B cell growth and increases immunoglobulin secretion and is also a key mediator in eosinophil activation. Interleukin 5 has long been associated with the cause of several allergic diseases including allergic rhinitis and asthma. Rat IL5 is a TH2 cytokine that is part of the hematopoietic family. Unlike other members of this cytokine family (namely IL3 and CSF2), this glycoprotein is a homodimer in its active form.

Interleukin-6 (IL6) is encoded by theIL6 gene in humans and acts as both a pro-inflammatory and anti-inflammatory cytokine. It is secreted by T-cells and macrophages to stimulate an immune response. Furthermore, it plays an essential role in the final differentiation of B-cells into Ig-secreting cells, which are involved in lymphocyte and monocyte differentiation. IL6 also induces myeloma and plasmacytoma growth. The human IL6 is a single nonglycosylated polypeptide chain containing 183 amino acids and it signals through a cell-surface type I cytokine receptor complex consisting of the ligand-binding IL6RG chain (CD126), and the signal- transducing component gp130 (also called CD130). The human IL6 is equally active on mouse and rat cells.

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Interleukin-6 (IL6) is a multifunctional protein that plays an important role in host defense, acute phase reactions, immune responses and hematopoiesis. IL6 is expressed by a variety of normal and transformed cells including T-cells, B-cells, monocytes/macrophages, fibroblasts, hepatocytes, keratinocytes, astrocytes, vascular endothelial cells and various tumor cells. The production of IL6 is upregulated by numerous signals, including mitogenic or antigenic stimulation, LPS, calcium ionophore, IL1, IL2, IFN, TNF, PDGF, and viruses. IL6 expression in monocytes is inhibited by IL4 and IL13.

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Interleukin-6 (IL6) is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T-cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL6 signals through the IL6 receptor system that consists of two chains, IL6R alpha and gp130.

Interleukin-6 (IL6) is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T-cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins and regulates bone metabolism. IL6 signals through the IL6 receptor system that consists of two chains: IL6Rα and gp130.

Interleukin-7 (IL7) is encoded by the IL7 gene and secreted by stromal cells in the red marrow and thymus. It binds to the IL7 receptor, a heterodimer consisting of IL7 receptor alpha and IL2 receptor gamma chains. IL7 stimulates the differentiation of hematopoietic stem cells into lymphoid progenitor cells. IL7 can also stimulate the proliferation of B-cells, T cells and NK cells (natural killer cells). Murine IL7 has approximately 61% amino acid sequence identity with human IL7, and both proteins exhibit cross-species activity. IL7 has been examined as an immunotherapy agent in many human clinical trials for various malignancies, along with its role in HIV-positive individuals.

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Interleukin-7 (IL7) is encoded by the IL7 gene and secreted by stromal cells in the red marrow and thymus. IL7 binds to the IL7 receptor, a heterodimer consisting of IL7 receptor alpha and IL2 receptor gamma chain. IL7 stimulates the differentiation of hematopoietic stem cells into lymphoid progenitor cells. It also stimulates the proliferation of B-cells, T-cells and NK cells. Murine IL7 has approximately 61% and 88% amino acid sequence identity with human and rat IL7, and both proteins exhibit cross-species activity. IL7 as an immunotherapy agent has been examined in many human clinical trials for various malignancies and during HIV infection.

Interleukin-7 (IL7) is encoded by the IL7 gene and secreted by stromal cells in the red marrow and thymus. It binds to the IL7 receptor, a heterodimer consisting of an IL7 receptor alpha chain and an IL2 receptor gamma chain. IL7 stimulates the differentiation of hematopoietic stem cells into lymphoid progenitor cells and also stimulates the proliferation of B-cells, T-cells and natural killer (NK) cells. Furthermore, IL7 as an immunotherapy agent has been examined in many human clinical trials for various malignancies including during HIV infection. Rat IL7 contains 129 amino acid residues and has three disulfide bonds. In addition, it has approximately 63% and 88% amino acid sequence identity with human and murine IL7 respectively.

Interleukin 8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. IL8 is also synthesized by endothelial cells, and then stored in vesicles. There are many receptors capable of binding to IL8; however, the receptors that have the greatest affinity are CXCR1 and CXCR2. As a member of the CXC chemokine family, IL8 is a player in the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils and T-cells. IL8 is often associated with inflammation and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.