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Interleukin-11 (IL11) is encoded by the IL11 gene and is a member of IL6 superfamily, which is distinguished based on its use of the common co-receptor gp130. IL11 is a multifunctional cytokine that was first isolated from bone marrow-derived stromal cells. IL11 receptor activation requires the formation of a complex that contains two IL11 molecules, two molecules of the ligand-binding IL11 RF subunit, and two molecules of the expressed cell signaling G-subunit, gp130. The functions of IL11 are that it directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells, and induces megakaryocyte maturation that results in increased platelet production.

Human interleukin-13 (IL13) is expressed by the IL13 gene located on chromosome 5 and is secreted by many cell types, especially T-helper type 2 (Th2) cells. The high solution form of IL13 is reported to be a monomer with two internal disulfide bonds that contribute to a bundled four F-helix configuration. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development and indicated an important role for IL13 in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages, and can also inhibit the expression of inflammatory cytokines such as IL1beta, TNF-alpha, IL6 and IL8. IL13 has also been shown to enhance B-cell proliferation, as well as induce isotype switching, which results in an increased production of IgE. Human, mouse and rat IL13 share a low percentage of homology, but have cross species activity.

Human Interleukin-13 (IL13) is expressed by the IL13 gene located on the chromosome 5. IL13 is a 112 amino acid protein containing a proposed 20 amino acid signal peptide making it 132 amino acids total, and shares approximately 30% amino acid sequence homology to human IL4. Additionally, the two cytokines exhibit overlapping biological activities. Human IL13 is produced by activated Th0, Th1-like Th2-like and CD8 T-cells. Similarly to IL4, IL13 has multiple effects on the differentiation of monocytes/macrophages, and can suppress their cytotoxic functions.

IL13 variant is a natural variant of the wild-type IL13 as it has a Q110 (glutamine) instead of an R110 (arginine), which is associated with increased risk for asthma development. At homozygosity, IL13V is associated with higher levels of total serum IgE in some allergic rhinitis patients.

Human interleukin-15 (IL15) is expressed by the IL15 gene located on chromosome 4. It shares approximately 97% and 73% sequence identity with simian and murine IL15, respectively. Both human IL15 and simian IL15 are active on murine cells. IL15 is secreted by mononuclear phagocytes, especially macrophages following infection by virus. It possesses a variety of biological functions that include the stimulation and maintenance of cellular immune responses, specifically the responses which regulate natural killer (NK) cell and T-cell activation and proliferation. In addition, IL15 shares many biological properties with IL2, including T, B and NK cell-stimulatory activities. IL15 signals through a complex composed of IL2/IL15 receptor beta chain. Although IL15 lacks sequence homology with IL2, it has been shown that both the beta and gamma chains of the IL2 receptor are utilized for IL15 binding and signaling. In addition, an IL15 specific binding protein has been cloned from a mouse T-cell clone.

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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.

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.

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 beta (IL1B) 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 IL1B bind to the same receptor and have similar but not identical biological properties.

Interleukin-1 receptor antagonist (IL1RN) is a member of the IL1 family. IL1RN is secreted by various types of cells including immune cells, epithelial cells and adipocytes, and is a natural inhibitor of the pro-inflammatory effect of IL1B. This protein also inhibits the activities of IL1A and modulates a variety of interleukin 1 related immune and inflammatory responses. IL4 and IL13 have been shown to amplify the stimulatory effect of IL1B on the production of soluble and intracellular forms of IL1RN. The regulated expression of IL1RN in various cell types has been shown to be influenced by cytokines. In synovial fibroblasts the synthesis of IL1RN is markedly enhanced by IL1, TNF-α, or PDGF. The protein shows 26% amino acid homology to IL1B and 19% homology to IL1A.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

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.

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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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.

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.

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.