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.

Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. IL8 is synthesized by endothelial cells, which stock IL8 in their storage vesicles. There are many receptors capable of binding to IL8; however, the molecules with the highest affinity to IL8 are receptors CXCR1 and CXCR2. As a member of the CXC chemokine family, one of the functions of IL8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils, and T-cells. IL8 (72a.a.) has a 5-10-fold higher activity on neutrophil activation compared to IL8 (77 a.a.). IL8 is often associated with inflammation, and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. There are many receptors capable of binding to IL8; however, the molecules with the highest affinity to IL8 are receptors CXCR1 and CXCR2. As a member of the CXC chemokine family, one of the functions of IL8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils and T-cells. IL8 (72a.a.) has a 5-10-fold higher activity on neutrophil activation, compared to IL8 (77 a.a.). IL8 is often associated with inflammation, and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

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.

Interleukin-8 (C-X-C motif chemokine 8) is coded by the interleukin 8 gene on chromosome 5 in Rhesus macaque (Macaca mulatta), which is not only 94% identical to human IL8, but also structurally and functionally similar with human IL8. IL8 also provides a valuable resource for a model of inflammation in primates.

Interleukin-9 (IL9) is encoded by the IL9 gene and is produced by T-cells and specifically by CD4+ helper cells. IL9 was originally identified as a cytokine found in the conditioned medium of a human T-cell leukemia virus type I (HTLVI) transformed T-cell line. IL9 functions through the IL-9 receptor, which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. IL9 can support the growth of IL-2 independent and IL4 independent helper T-cells. Human IL9 has approximately 56% amino acid sequence identity with murine IL9. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

Interleukin-9 (IL9) is encoded by the IL9 gene and is produced by T-cells and specifically by CD4+ helper cells. IL9 was originally identified as a cytokine found in the conditioned medium of a human T-cell leukemia virus type I (HTLVI) transformed T-cell line. IL9 functions through the IL-9 receptor, which activates different signal transducer and activator (STAT) proteins and thus connects this pleiotropic cytokine to various biological processes. IL9 can support the growth of IL2 independent and IL4 independent helper T-cells. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

Thymic stromal lymphopoietin (TSLP) is a hemopoietic protein belonging to the cytokine family and is known to play an important role in the maturation of T cell populations through activation of antigen presenting cells. It is mainly expressed in tissues, including heart, liver and prostate. TSLP signals through a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor and the IL7R alpha chain. Like IL7, TSLP induces phosphorylation of STAT3 and STAT5, but uses kinases other than the JAKs for activation. After binding STAT5, phosphorylation is induced which results in the expression of downstream transcription factors. TSLP enhances the maturation of CD11c+ dendritic cells and induces allergic inflammation by directly activating mast cells. TSLP’s expression is linked to many disease states including asthma, inflammatory arthritis, atopic dermatitis, and eczema and other allergic states but the factors which induce the activation of TSLP release are not clearly defined. Human TSLP shares approximately 43 % amino acid sequence identity with mouse TSLP.