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Interleukin 1 beta (IL-1β) is synthesised as an inactive precursor protein or pro-IL-1β. This precursor is cleaved intracellularly by caspase 1 (IL-1β convertase) to form the active form of the protein that is later secreted (Allan et al.). IL-1β binds to IL-1 receptor and activates intracellular signaling via the MAPK or NF-kB pathway. IL-1β is released by monocytes, tissue macrophages, and dendritic cells in response to infection or injury and induces expression of acute-phase proteins. It also promotes the infiltration of inflammatory and immunocompetent cells from the circulation into the extravascular space and affected tissues, by stimulating the expression of adhesion molecules on endothelial cells. IL-1β also affects other immune cells; for example, it co-stimulates T cell functions together with antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner. Mice deficient in IL-1β do not show phenotypical differences from wild-type mice; however, they have a reduced response to inflammation, suggesting that IL-1β plays a key role in inflammatory diseases (Dinarello).

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Macrophage inflammatory protein-1 alpha (MIP-1 alpha), also known as CCL3, is a member of the CC family of chemokines and is most closely related to CCL4 or MIP-1 beta. Mouse MIP-1 alpha signal through CCR1, CCR3, CCR5, and D6 receptors (Menten et al.). MIP-1 alpha exhibits a variety of proinflammatory activities in vitro, including leukocyte chemotaxis, cytokine production, and mast cell activation, and it inhibits the proliferation of hematopoietic stem cells in vitro and in vivo (Cook). MIP-1 alpha plays a critical role in macrophage recruitment into wounds and in tissue repair (DiPietro et al.). It has been demonstrated that blockade of the CCL3/MIP-1 alpha-CCR1 pathway blocks the recruitment of CCR1-expressing CD4+ T cells to the liver, showing a therapeutic potential for treating T cell-mediated liver diseases (Ajuebor et al.).

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Platelet-derived growth factor (PDGF) is a dimeric glycoprotein consisting of two disulfide bridge-stabilized polypeptide chains, A and B, which are assembled as heterodimers (PDGF-AB) or homodimers (PDGF-AA and PDGF-BB) (Fretto et al.; Westermark and Heldin). PDGF signals through the receptor tyrosine kinases PDGFRalpha and PDGFRbeta. PDGF-induced migration has been shown to involve MEK/ERK, EGFR, Src, and PI3K/Akt signaling pathways (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin- like fibroblasts, glial cells, and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-BB is secreted by osteoblasts to induce mesenchymal stem cell migration and angiogenesis. It has also been shown that PDGF-BB is secreted by preosteoclasts during bone modeling and remodeling to induce angiogenesis and thus proper osteogenesis (Xie et al.). This product is animal component-free.

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Interleukin 1 alpha (IL-1α) is a member of the IL-1 family and a dual-function cytokine. Both the unprocessed precursor and a processed IL-1α protein signal through IL-1 receptor type 1 (IL-1R1). Various cells, including keratinocytes, thymic epithelium, hepatocytes, endothelial cells, fibroblasts, and the epithelial cells of mucous membranes have high levels of intracellular IL-1α precursor, which is also expressed on the surface of monocytes and B lymphocytes (Netea et al.). IL-1α recruits infiltrating cells to a site of injury during necrosis and plays an important role during processes of sterile inflammation (Rider et al.; Cohen et al.). During hypoxia, IL-1α contributes to angiogenesis (Carmi et al.). IL-1α is produced by microglia-like cells after ischemic brain injury, which contributes to the inflammation (Luheshi et al.).

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Mediate calcium phosphate clearance and prevent ectopic calcification with fetuin A, a plasma glycoprotein that forms soluble complexes with calcium and phosphate (Heiss et al.; Price and Lin). Belonging to the cystatin superfamily of cysteine protease inhibitors (Brown and Dziegielewska), fetuin A has also been shown to play a role in lipid transport, acting as a carrier (Kumbla et al.). In cell-based assays, it has been suggested that fetuin A protects against lethal systemic infection through the inhibition of high mobility group box 1 (HMGB1) protein accumulation and release (Li et al.). Fetuin A acts as a natural antagonist against specific TGF-β and BMP signaling proteins, blocking osteogenic differentiation of rat bone marrow cells (Demetriou et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, fetuin A from STEMCELL comes lyophilised with ≥94% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Monokine induced by interferon-gamma (MIG), or CXCL9, is a member of the CXC chemokine family. MIG is closely related to two other chemokines: CXCL10 and CXCL11, all of which signal through the CXCR3 receptor (Ding et al.). MIG is secreted by a variety of immune cells including T cells, NK cells, dendritic cells, macrophages, and eosinophils, as well as non-immune cells including hepatic stellate cells, preadipocytes, thyrocytes, endothelial cells, tumor cells, fibroblasts, and glial cells of the central nervous system. MIG has also been shown to act as a chemoattractant for activated T cells and for tumor-infiltrating leukocytes (TILs), but not for neutrophils or for monocytes. MIG has also been reported to be both a tumor suppressor and tumor promoter in various types of cancer.

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Heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) is a member of the EGF family (Nishi and Klagsbrun). HBEGF promotes blastocyst adhesion to the uterine wall (Iwamoto and Mekada). It also plays a role in smooth muscle cell hyperplasia and brain injury (Nishi and Klagsburn). HBEGF produced by CD4+ T cells promotes wound healing by stimulating migration and proliferation of keratinocytes, fibroblasts, and smooth muscle cells (Blotnick et al.). It binds to EGFR, ErbB4, ErbB2, and ErbB3, activating the PI3K/AKT signaling cascade (Iwamoto and Mekada). HBEGF is produced in a variety of cells, where it contributes to physiological and pathological processes. HBEGF is overexpressed in ovarian, breast, gastric, colorectal, pancreatic, and endometrial cancers, which likely contributes to pathogenesis (Miyata et al.).

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Use Interleukin 37 (IL-37) to inhibit the expression of inflammatory cytokines, such as IL-6, MIP-1α, MIP-1β, and TNF-α, in a MAPK-dependent manner (Qi et al.). A secreted protein belonging to the interleukin-1 cytokine family, IL-37 acts as an anti-inflammatory alarmin, with predominant expression in monocytes, and constitutive secretion by myeloid dendritic cells (Rudloff et al.). IL-37 has been shown to limit inflammation in human blood M1 macrophages by binding to extracellular surface receptors, requiring IL-1R8 as a coreceptor (Li et al.). It also has protective effects against obesity-induced inflammation and insulin resistance, reducing adipogenesis and activating AMPK signaling both in vitro and in vivo (Ballak et al.). In humans, the IL-37 gene undergoes alternative splicing, resulting in multiple isoforms of the protein (Boraschi et al.). For consistency and reproducibility across your applications, Interleukin 37 from STEMCELL comes lyophilised with ≥93% purity.

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Apolipoprotein H (apo H) has been shown to promote the coagulation of blood platelets by inhibiting thrombomodulin complex and inactivating protein C (Keeling et al.), but can also act as an anticoagulant by binding thrombin and inhibiting its procoagulant effects (Pozzi et al.). Belonging to the lipid-binding apolipoprotein family, within the lipocalin superfamily, apo H is a protein constituent of plasma, with a high affinity for negatively charged phospholipids. The structure of apo H reveals four N-terminal complement control protein (CCP) modules, also known as 'sushi' domains, and a distinct fifth C-terminal domain with four antiparallel beta sheets, two alpha-helices, and an extended loop (Schwarzenbacher et al.). Apo H is the main antigen implicated in antiphospholipid syndrome (APS), an autoimmune condition involving pregnancy complications and vascular thrombosis (Brusch). Studies have also reported that Apo H is involved in the progression of atherosclerosis (Harats and George). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apolipoprotein H from STEMCELL comes lyophilised with ≥93% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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Interferon-gamma (IFN-γ), also known as type II interferon, is produced by T and NK cells, and in smaller amounts by dendritic cells and macrophages. IFN-γ is controlled by cytokines such as IL-12 and IL-18 secreted in response to infection (Schroder et al.). IFN-γ binds to a receptor complex and initiates signal transduction via the JAK/STAT pathway; this culminates in the transcription and activation of many genes that control a diverse array of immunological functions (de Weerd and Nguyen; Krause et al.). IFN-γ stimulates the antimicrobial and anti-tumor activity of macrophages, NK cells, and neutrophils (Billiau and Matthys) by promoting the activation of microbial effector functions such as production of reactive oxygen species, nitric oxide, and complement (Schroder et al.). IFN-γ enhances MHC class I and II expression in dendritic cells and mononuclear phagocytes, as well as the production of IL-12 by dendritic cells. In B cells, IFN-γ stimulates survival and growth in both mouse and human cells, and redirects B cells from proliferation towards differentiation. IFN-γ favors the development of Th1 vs Th2 cells and stimulates monocyte differentiation and function (Schroder et al.).

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Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes the proliferation and differentiation of hematopoietic progenitor cells and the generation of neutrophils, eosinophils, and macrophages. In synergy with other cytokines such as stem cell factor, IL-3, erythropoietin, and thrombopoietin, it also stimulates erythroid and megakaryocyte progenitor cells (Barreda et al.). GM-CSF is produced by multiple cell types, including stromal cells, Paneth cells, macrophages, dendritic cells (DCs), endothelial cells, smooth muscle cells, fibroblasts, chondrocytes, and Th1 and Th17 cells T cells (Francisco-Cruz et al.). The receptor for GM-CSF (GM-CSFR) is composed of two subunits: the cytokine-specific α subunit (GMRα; CD116) and the common subunit βc (CD131) shared with IL-3 and IL-5 receptors (Broughton et al.). GM-CSFR is expressed on hematopoietic cells, including progenitor cells and immune cells, as well as non-hematopoietic cells. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.). Recombinant rat GM-CSF is reactive with mouse cells (Oaks et al.; Vandenabeele et al.).

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Interferon-alpha (IFN-α) is a type I interferon, produced by virus infected cells, and is released as a soluble factor to initiate antiviral responses (Isaacs and Lindenmann). IFN-α2 is the most potent IFN-α used in fundamental research and in most clinical applications. The best known IFN-α2 subvariants, 2A and 2B, differ by only one or two amino acids at positions 23 and/or 34 of the mature protein (von Gabain et al.). Type I IFNs exert potent antitumor activity by increasing the cytotoxic activity of NK and T cells, as well as inhibiting the proliferation of cancer cells (Paul et al.). Additionally, it has been shown that proinflammatory IFN-α modulates the function of B cells in patients with systemic lupus erythematosus (Chang et al.) and pegylated form of IFN-α 2A and 2B has implications in the treatment of Hepatitis C (Foster et al.).

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GRO (growth-regulated oncogene)-beta or CXCL2 is a member of the CXC family, which plays an integral role in recruitment and activation of neutrophils and basophils in response to tissue injury and microbial infection. GRO-beta and GRO-gamma are closely related to GRO-alpha and share 90% and 86% amino acid sequence homology, respectively, with GRO-alpha. Receptor-binding studies have demonstrated that GRO-alpha, -beta, and -gamma signal mainly through G protein-coupled receptors CXCR1 and CXCR2 (Ahuja and Murphy). GRO-beta is expressed in epithelial cells, monocytes, fibroblasts, and melanocytes and is further induced during inflammatory, epithelialization, and angiogenic processes, for example during the wound healing process of human burn wounds (Zaja-Milatovic and Richmond). GRO-beta also stimulates mitogenesis in certain human melanoma cells (Unemori et al.).

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Fibroblast growth factor 18 (FGF-18) is a growth factor and member of the FGF subfamily. FGF-18 is most similar to FGF-8 and FGF-17, and is secreted in adult lung and developing tissues (Ohbayashi et al.). FGF-18 signals through FGF receptor 3 (FGFR3) to regulate proliferation, differentiation, and matrix production of articular and growth plate chondrocytes in vivo and in vitro (Davidson et al.). FGF-18 has skeletal functions and protects articular cartilage by gene expression profiling and regulates proliferation and differentiation of midline cerebellar structures (Mori et al.). Also, recombinant human FGF-18 has been shown to effectively regulate hair growth (Song et al.).

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Use sclerostin to alter bone remodeling homeostasis, where it inhibits bone formation in vivo and in vitro, likely through Wnt/β-catenin signaling cascades (Ellies et al.; Lin et al.). Sclerostin is a member of the cerberus/DAN family of glycoproteins whose members share a C-terminal cysteine-knot-like (CTCK) domain. Highly expressed in bone and cartilage, as well as in kidney, and liver tissues (Weivoda et al.), this osteoclast-derived BMP antagonist binds BMP6 and BMP7 with high affinity, and binds BMP2 and BMP4 with a lower affinity (Kusu et al.). Mutations in the SOST gene have been associated with sclerosteosis (Brunkow et al.), van Buchem disease (Staehling-Hampton et al.), and bone dysplasia disorders, characterized by increased bone density. This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Human Interleukin 4 (IL-4) is important for immune responses to helminth infection as well as in allergic responses (Olpihant et al.). The IL-4 receptor consists of a heterodimer of IL-4Ra and common gamma chain. IL-4 receptor engagement leads to the activation of JAK1/3 and the recruitment of STAT6 and IRS1/2 (Nelms et al.). IL-4 drives immunoglobulin class switching in B cells (to IgE, IgG4), mast cell hyperplasia, mucus production, and the differentiation of naïve T cells into Th2 cells, which produce IL-4, IL-5, IL-10, and IL-13 (Bao et al.; Nelms et al.; Olpihant et al.). In addition to Th2 cells, IL-4 is produced by CD4+ NK T cells, γ/δ T cells, activated basophils, eosinophils, and mast cells. Human IL-4 does not cross-react with mouse cells (Park et al.).

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Fibroblast growth factor 4 (FGF-4) is a member of the FGF superfamily (Beenken and Mohammadi). FGF-4 is expressed in pluripotent stem cells and is implicated in various stages of development and morphogenesis in a variety of organisms (Kosaka et al. 2009). FGF-4 has been shown to have an ability to promote neural stem cell proliferation and neuronal differentiation in the postnatal brain (Kosaka et al. 2006). FGF-4 has also been shown to increase the proliferation rate of mesenchymal stem cells (Farré et al.). FGF-4 supports the maintenance and self-renewal properties of human embryonic stem cells and also promotes the proliferation of these cells (Mayshar et al.). In the mouse, the Fgf4 gene also supports proliferation of the inner cell mass (ICM) and postimplantation embryos (Feldman et al.).

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Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including mast cells, basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Fung et al.; Metcalf et al.; Broughton et al.). IL-3 is produced by activated T cells, and has a physiological role in inflammation and allergies by promoting the secretion of inflammatory mediators such as histamine, IL-4, and IL-6 by mast cells, basophils and eosinophils. The mouse IL-3 receptor consists of a unique alpha-subunit (CD123) and two beta subunits, one specific for IL-3 (βIL-3), the other shared with the receptors for IL-5 and GM-CSF (beta common chain, βc or CD131). IL-3 binding to heterodimeric receptors containing the alpha subunit and one of either beta subunits activates JAK/STAT, MAPK, and PI3K signaling pathways (Scott and Begley).

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Tumor necrosis factor-α (TNF-α) is a pro-inflammatory cytokine that activates NF-κB, MAPK, and PI3K/AKT pathways. Activated T cells and macrophages are the primary producers of TNF-α in response to inflammation and infectious conditions. Many other cell types have been shown to produce TNF-α, among them B cells, NK cells, mast cells, neutrophils, dendritic cells, microglia, endothelial cells, smooth muscle cells, cardiomyocytes, and fibroblasts. TNF-α has cytotoxic effects on cancer cells in vitro by stimulating anti-tumor immunosuppressive responses. TNF-α stimulates expression of E- and P-selectins, thus facilitating adhesion of neutrophils, monocytes, and memory T cells to activated platelets and endothelial cells (Zelová andamp; Hosek). Other effects of TNF-α include vasodilatation and edema formation.

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Fractalkine (CX3CL1) is a unique chemokine belonging to the CX3C family, and is characterized by a C-X3-C cysteine motif within the chemokine domain, near the amino terminus of the protein (Bazan et al.). The chemokine domain is connected to an extended mucin-like stalk, followed by a transmembrane region, and a C-terminal intracellular domain (Imai et al.; Jones et al.). The protein signals through interaction with a single receptor, CX3CR1, expressed on monocytes, natural killer cells, T cells, microglia, and smooth muscle cells. Fractalkine is upregulated in endothelial cells by inflammatory signals and is synthesized as a membrane-bound molecule that mediates cell migration and adhesion (White and Greaves). Cleavage at the base of the stalk by metalloproteinases generates a soluble chemokine, which functions as a potent chemoattractant of target cells (Garton et al.; Apostolakis and Spandidos). Fractalkine has been implicated in pathology of inflammatory diseases, such as atherosclerosis and other vascular diseases, and has anti-apoptotic functions (White and Greaves).

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Interleukin 10 (IL-10) is the founding member of the IL-10 family of class II cytokines. All of the IL-10 cytokine family members have a four-helix bundle consisting of α-helical folds. Upon binding to its receptor, IL-10 activates signaling through JAK1 and STAT3. It is produced by dendritic cells, macrophages, and CD4 T cells, as well as mast cells, NK cells, neutrophils, and B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the expression of pro-inflammatory cytokines and promote healing processes, and is important for the function of T regulatory cells. IL-10 also enhances B cell proliferation, immunoglobulin secretion, and class II MHC expression, while IL-10 produced by macrophages inhibits activation of neighboring macrophages, thus allowing a level of self-regulation (Ouyang et al.). This product is animal component-free.

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Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Yang et al.; Dorssers et al.; Broughton et al.). IL-3 is produced by activated T cells and has a physiological role in inflammation and allergies by promoting the secretion of inflammatory mediators such as histamine, IL-4, and IL-6 by basophils and eosinophils (Broughton et al.). The IL-3 receptor consists of a unique alpha subunit (CD123) and a beta common subunit (βc or CD131) that is shared with the receptors for IL-5 and GM-CSF, and is the principal signal transduction subunit for these cytokines. IL-3 binding to the heterodimeric receptor activates JAK/STAT, MAPK, and PI3K signaling pathways (Woodcock et al.).

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Fibroblast growth factor 7 (FGF-7) is a member of the FGF family, and acts exclusively through a subset of FGF receptor isoforms expressed predominantly by epithelial cells (Finch and Rubin). FGF-7 seems to act specifically on epithelial cells and stimulates proliferation, migration, and differentiation of these cells, and also participates in epithelial protection and repair both in vitro and in vivo (Finch and Rubin; Werner). In contrast, FGF-7 is produced solely by cells of mesenchymal origin, and functions as a paracrine mediator of mesenchymal-epithelial communication (Rubin et al.). FGF-7 has also been shown to supplement several wound-healing properties of bioengineered skin (Erdag et al.) and to induce autophagy in human keratinocytes (Belleudi et al.). Additionally, FGF-7 has a role in the differentiation of pluripotent stem cell to endodermal pancreatic-like insulin-producing cells and thymic epithelial cells (Inami et al.; Niu et al.). This product is animal component-free.

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Modulate prostaglandin metabolism with 15-hydroxyprostaglandin dehydrogenase (15-PGDH). 15-PGDH catalyses the reversible oxidation of the 15-hydroxyl group in prostaglandins, resulting in inactivated metabolites (Ensor and Tai), it can act on a variety of prostaglandins as substrates in a NAD+ dependent manner (Cho et al.). As prostaglandins can have a range of effects on cellular processes, 15-PGDH is of considerable importance in drug development. In vitro and in vivo studies suggest 15-PGDH has tumor suppressive activity and is downregulated in certain cancers (Na et al.).15-PGDH belongs to the short-chain dehydrogenases/reductases (SDR) family; its primary structure indicates 20% homology with other SDRs, with some conserved amino acid residues (Krook et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apo M from STEMCELL comes lyophilised with ≥89% purity.

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Interleukin 1 receptor antagonist (IL-1RA) is a member of the IL-1 family that binds to IL-1 receptors but does not induce any intracellular signaling (Arend et al.). IL-1RA is a natural regulator of IL-1’s biological activity. It binds to the IL-1 receptors with similar affinity as IL-1, thereby inhibiting the proinflammatory activities of IL-1ɑ and IL-1ꞵ (Kinne et al.). In particular, mesenchymal stem cells have been shown to enhance tissue repair in an IL-1RA-dependent manner through the suppression of IL-1ꞵ production in dermal macrophages and enhanced expansion of immunosuppressive regulatory T cells in the skin (Harrell et al.). IL-1RA has also been shown to help in the treatment of rheumatoid arthritis (Cutolo), sepsis, asthma (Mao et al.), and inflammatory bowel diseases (Dosh et al.). This product is animal component-free.

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Fibroblast growth factor acidic (FGF-acidic), also known as FGF-1, is a potent activator of DNA synthesis, cell proliferation, and chemotaxis and is known to play numerous roles in development, regeneration, and angiogenesis (Jaye et al.; Galzie et al.; Presta et al.). FGF-acidic is produced by multiple cell types and is capable of activating all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It is found in large quantities in the brain, but is also expressed in hepatocytes, vascular smooth muscle cells, neurons of the CNS, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelial cells, and pituitary basophils and acidophils. FGF-acidic is secreted as a disulfide-linked homodimer and is stored in complex with heparan sulfate, a requirement for its interaction with FGF receptors (Guerrini et al.; Mohammadi et al.). Internalized FGF-acidic signals through protein kinase C and promotes cell survival by inhibiting p53 and proapoptotic signaling (Bouleau et al.).

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Interleukin 21 (IL-21) is a pleiotropic cytokine that is composed of four α-helical bundles and primarily produced by natural killer T (NKT) cells, T follicular helper (Tfh) cells, and Th17 cells (Spolski and Leonard 2008). IL-21 signals via receptor heterodimerization of IL-21 receptor and IL-2 receptor subunit gamma (IL-2RG or CD132), both of which have a common gamma-chain subunit and activate the JAK/STAT, MAPK, and PI3K pathways (Parrish-Novak et al.; Ozaki et al. 2000; Spolski and Leonard 2014). IL-21 has been shown to have a critical role in regulating immunoglobulin production and differentiation of the pro-inflammatory Th17 population of cells (Ozaki et al. 2002; Nurieva et al.). Additionally, IL-21 specifically sustains CD8+ T cell effector activity and provides a mechanism of CD4+ T cell help during chronic viral infection (Elsaesser et al.). IL-21 signaling was also found critical for the development of type 1 diabetes in non-obese diabetic (NOD) mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.).

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Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to the ST2 receptor and activates NF-kB and MAPK pathways. IL-33 is expressed by epithelial cells, smooth muscle cells, and fibroblasts in various tissues and organs, as well as resting basophils, mast cells, eosinophils, natural helper cells, group 2 innate lymphoid cells, dendritic cells, and activated macrophages (Schmitz et al.; Yasuda et al.). It contributes to allergic inflammation by stimulating production of the cytokines IL-4, IL-5, and IL-13 in Th2 cells, and stimulates host defense against microbial and viral infections (Liew; Yasuda et al.). In the central nervous system, IL-33 is produced by endothelial cells and astrocytes. It induces proliferation of microglia and mediates production of pro-inflammatory cytokines (Yasuoka et al.).

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Interleukin 13 (IL-13) is a type I cytokine, and signals through type I cytokine receptors to activate JAK/STAT and IRS-1/IRS-2 pathways. IL-13 is produced by T cells and innate lymphoid cells (Pulendran and Artis) and it inhibits production of pro-inflammatory cytokines, prostaglandins, and reactive oxygen and nitrogen species by monocytes and macrophages (Hershey). Unlike human B cells, IL-13 has no effect on mouse B cell development and function. IL-13 promotes eosinophil survival, activation, and recruitment, and also activates mast cells (Hershey). IL-13 regulates gastrointestinal parasite expulsion, airway hyperresponsiveness, allergic inflammation, tissue eosinophilia, goblet cell hyperplasia, intracellular parasitism, tissue remodeling, tumor cell growth, and fibrosis. IL-13 induces hypercontractility of smooth muscles by directly acting on the muscle cells as well as the enteric nerves (Wynn).