Human interleukin-16 (IL16) is also called lymphocyte chemoattractant factor (LCF) and it has three isoforms, which are cleaved from preinterleukin16. IL16 is mostly secreted by lymphocytes, epithelial cells, eosinophils and CD8+ T-cells. IL16 signals through the CD4 receptor, and has many functions, which include the induction of the IL2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions, and many more. Furthermore, recombinant human IL16 (121 a.a.) contains 121 amino acid residues and shares 85% amino acid sequence identity with murine IL16.

Human interleukin-16 (IL16) is also called lymphocyte chemoattractant factor (LCF), and it has three isoforms, which are cleaved from pre-interleukin-16. IL16 is mostly secreted by lymphocytes, epithelial cells, eosinophils and CD8+ T-cells. IL16 signals through the CD4 receptor, and has many functions, which include the induction of the IL2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions, and many more. Furthermore, recombinant human IL16 (130 a.a.) contains 130 amino acid residues and shares 85% amino acid sequence identity with murine IL16.

Interleukin-16 (IL16) is also called lymphocyte chemoattractant factor (LCF) and is mostly secreted by lymphocytes, epithelial cells, eosinophils and CD8+ T-cells. It has many functions, including the induction of IL2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, and the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions. IL16 produces its signal through the CD4 receptor. Furthermore, recombinant murine interleukin-16 contains 118 amino acid residues and shares about 85% amino acid sequence identity with different isoforms of human IL16.

Interleukin-16 (IL16), also called lymphocyte chemoattractant factor (LCF), is predominately secreted by lymphocytes, epithelial cells, eosinophils, and CD8+ T-cells. It has many functions, including the induction of IL-2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, and the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions. IL16 signals through the CD4 receptor. Furthermore, recombinant rhesus macaque IL16 contains 121 amino acid residues and shares 95% and 85% amino acid sequence identity with human and murine IL16, respectively.

Human interleukin-17A (IL17A) is encoded by the IL17A gene located on chromosome 6, and belongs to the IL17 family that contains IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. All of the members of the IL17 family have a similar protein structure, which includes four highly conserved cysteine residues that are critical to their 3 dimensional shape. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers, and mature IL17 contains one potential N-linked glycosylation site. At the amino acid level, IL17 exhibits 63% amino acid identity with mouse IL17. However, there is no reported sequence similarity to any other known cytokines. IL17 is a T-cell expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of the herpesvirus, Saimiri. High levels of human IL17 were induced from primary peripheral blood CD4+ T-cells upon stimulation, which can induce stromal cells to produce proinflammatory and hematopoietic cytokines.

Rat Interleukin 17A (IL17A) belongs to the IL17 family that contains IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. All of the members of the IL17 family are proinflammatory cytokines that share four conserved cysteine residues, but diverge at the N-terminus. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers, and mature IL17 contains one potential N-linked glycosylation site. IL17 is a T-cell expressed pleiotropic cytokine that regulates the activities of NF-kappaB and mitogen-activated protein kinases, and can stimulate the expression of IL-6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO).

IL17B, also named IL20, NIRF and ZCYTO7, belongs to the IL17 family and it stimulates the release of tumor necrosis factor alpha (TNF-α) and IL1-beta from the monocytic cell line THP-1. IL17B mRNA is expressed in adult pancreas, small intestine, and stomach. The IL17 family is comprised of at least six proinflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL17 family members are glycoproteins secreted as dimers that induce local cytokine production and recruit granulocytes to sites of inflammation. IL17B binds the IL17B receptor, but not the IL17 receptor; it is most homologous with IL17D, which is expressed by resting CD4+ T cells and CD19+ B cells. Immunohistochemical analysis of several nerve tissues indicates that this cytokine is primarily localized to neuronal cell bodies.

Human interleukin-17F (IL17F) is encoded by the IL17F gene located on chromosome 6, and belongs to the IL17 family, which contains: IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. IL17F shares 50% homology to the crystal structure of IL17A, and is expressed by activated T-cells. IL17 can stimulate the production of other cytokines such as IL6, IL8 and granulocyte colony-stimulating factor. IL17 also plays a role in the proliferation of PBMCs (peripheral blood mononuclear cells) and T-cells, the regulation of cartilage matrix turnover, and the inhibition of angiogenesis.

Human interleukin-19 (IL19) is encoded by the IL19 gene, which is located on chromosome 1. The protein belongs to the IL10 family of interleukins, which includes: IL10, IL20, IL22, IL24, and IL26. As a monomer made of seven amphipathic helices, IL19 has a helical bundle and shares the same cell surface receptor (IL20R) with IL20 and IL24. IL19 may play an important roles in inflammatory responses because it promotes the upregulation of IL6 and TNF-α, induces apoptosis, and activates the autoantibody production in B-cells.

Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological, hematopoietic activities, and plays one of the central roles in the regulation of the immune responses. Both IL1A and IL-1B bind to the same receptor and have similar biological properties. Among various species, the amino acid sequence of mature IL1A is conserved 60% to 70% and human IL1A has been found to be biologically active with murine cell lines.

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Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar biological properties. These cytokines have a broad range of activities including stimulation of thymocyte proliferation by inducing IL2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1B is a secreted cytokine, IL1A is predominantly a cell associated cytokine.

Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological and hematopoietic activities, and plays one of the central roles in the regulation of immune responses. Both IL1A and IL1B bind to the same receptor and have similar but not identical biological properties. Recombinant rat IL1A contains 150 amino acids, which is a single nonglycosylated polypeptide.