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Interleukin 19 (IL-19) is a member of the IL-10 cytokine family and is produced by keratinocytes, B cells, and monocytes (Romer et al.; Wolk et al.). Expression of IL-19 can be induced by granulocyte-macrophage colony-stimulating factor (GM-CSF) or lipopolysaccharide (LPS; Gallagher et al.). IL-19 is considered to be a proinflammatory cytokine, as it upregulates IL-6 and tumor necrosis factor alpha (TNF-α; Liao et al. 2002). IL-19 binds the IL-20 receptor complex (IL-20R) which comprises IL-20R alpha and IL-20R beta to activate the STAT3 pathway (Dumoutier et al.). IL-19 also induces T-helper cell differentiation towards a Th2 response, resulting in the production of IL-10 and additional IL-19 (Liao et al. 2002; Liao et al. 2004). IL-19 has been implicated in aging, vascular disease, Type I diabetes, and rheumatoid arthritis.

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Basic fibroblast growth factor (bFGF) is a prototypic member of the fibroblast growth factor family. Cytokines in the FGF family possess broad mitogenic and cell survival activities (Folkman and Klagsbrun; Kimelman and Kirschner) and are involved in a variety of biological processes including cell proliferation, differentiation, survival, and apoptosis (Folkman and Klagsbrun; Klagsbrun; Rifkin and Moscatelli). bFGF has the β-trefoil structure (Ponting and Russell), binds to the four FGF receptor (FGFR) family members, and activates JAK/STAT, PI3K, ERK1/2, and other receptor tyrosine kinase (RTK) signaling pathways. It supports the maintenance of undifferentiated human pluripotent stem cells (Xu et al.; Kang et al.), stimulates human pluripotent stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.). This version of bFGF is the full-length bFGF protein encoded by the human FGF2 gene consisting of 154 amino acid residues. This product is animal component-free.

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Use omentin for the maintenance of insulin sensitivity and metabolism, decreasing levels of this adipokine have been associated with obesity, insulin resistance, and diabetes (Tan et al.). Studies have suggested that omentin may have protective effects against atherosclerosis, arterial calcification, and myocardial injury through AMP-activated protein kinase (AMPK) and Akt-dependent mechanisms (Xu et al., Kataoka et al.). Through regulation of Sirt1-dependent p53 deacetylation, omentin can inhibit proliferation and induce apoptosis in hepatocellular carcinoma cells (Zhang and Zhou). Omentin is mainly produced by visceral adipose tissue, but is also expressed in the small intestine, colon, mesothelial cells, vascular cells, and plasma (Watanabe et al). Protein sequence analysis has shown that omentin comprises 313 amino acids, with a secretory signal sequence and fibrinogen-related domain (Yang et al.). For consistency and reproducibility across your applications, Omentin from STEMCELL comes lyophilised with ≥90% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤5,0 EU/μg protein.

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Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to heterotrimeric receptors consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). High IL-2 levels in serum are associated with progression of scleroderma, rheumatoid arthritis, and gastric and non-small cell lung cancer, though no known disease can be directly attributed to the lack or excess of IL-2 (Gaffen and Liu).

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Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf and Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilisation of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways. This product is animal component-free.

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Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf andamp; Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilisation of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.

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Interleukin 31 (IL-31), a four-helix bundle inflammatory cytokine, belongs to the IL-6 cytokine family which includes IL-6, oncostatin M, leukemia inhibitory factor (LIF), and cardiotrophin-1 ( Dillon et al.). IL-31 signals through a heterodimer composed of IL-31RA (also known as gp130-like receptor or GPL) and the oncostatin-M receptor (OSMR), both of which are expressed on monocytes (Diveu et al.; Ghilardi et al.), epithelial cells (Ip et al.), and keratinocytes (Kato et al.). Signaling through the GPL/OSMR complex activates the JAK/STAT, RAS/ERK, and PI3K/AKT signaling pathways, resulting in the downstream activation of STAT1, STAT3, and STAT5 transcription factors (Cornelissen et al.; Dambacher et al.; Dillon et al.; Ip et al.). IL-31 responses have been associated with allergic responses and inflammatory skin diseases including atopic dermatitis (Cornelissen et al.; Gangemi 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 (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.).

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Fibroblast growth factor 10 (FGF-10) is a member of the fibroblast growth factor (FGF) family predominantly expressed by mesenchymal fibroblasts during embryonic development (Emoto et al.; Igarashi et al.). It binds with high affinity to fibroblast growth factor receptor 2-IIIb (FGFR2-IIIb), and also has a weaker affinity for FGFR1-IIIb (Beer et al.). FGF-10 and FGF-7 have similar receptor binding properties and target cell specificities but are differentially regulated by components of the extracellular matrix (Emoto et al.; Igarashi et al.). FGF-10 has been shown to mediate epithelial-mesenchymal interactions, which are essential to lung development (Sekine et al; Ware and Matthay). FGF-10 also has a role in mobilisation and proliferation of lung-resident mesenchymal stem cells (MSCs) and protection and repair against acute lung injury (Tong et al.; Ware and Matthay), as well as endodermal differentiation of human pluripotent stem cells to insulin-producing pancreatic-like cells (Takeuchi et al.).

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Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells, however mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.). This product is animal component-free.

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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, NO intermediates, 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.). This product is animal component-free.

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Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to a heterotrimeric receptor consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). Targeted deletions of the IL-2 gene in mice resulted in development of autoimmune hemolytic anemia, followed by ulcerative colitis. Similar effects were observed in mice that were deficient in IL-2 receptor α (Gaffen and Liu).

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Persephin is a neurotrophic factor that belongs to the glial cell line-derived neurotrophic factor (GDNF) family. Persephin shares a large degree of structural similarity to GDNF, artemin, and neurturin, and has overall neuroprotective activity. Persephin signals through GRFα4 (glycosylphosphatidylinositol (GPI)-linked GDNF receptor family member) which signals through the receptor tyrosine kinase RET. Unlike GDNF and neurturin, persephin only promotes the growth and survival of central dopaminergic and motor neurons, but not peripheral neurons (Milbrandt et al.). In vitro, persephin only promotes survival of neurons that co-express GPI-linked GRFα4 and RET (Enokido et al.; Lindahl et al.). Mice lacking persephin showed increased cell death after cerebral ischemia, however administration of persephin before ischemia dramatically reduced neuronal cell death (Tomac et al.).

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The platelet-derived growth factor (PDGF) family has five heparin-binding members that assemble into four homodimers (PDGF-AA, PDGF-BB, PDGF-CC, and PDGF-DD) and one heterodimer (PDGF-AB; Fretto et al.; Li and Eriksson). PDGF signals through the receptor tyrosine kinases PDGFRα and PDGFRβ. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src, and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin, such as 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.).

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Interleukin 6 receptor (IL-6R) alpha is a type I transmembrane glycoprotein that forms a complex with type I transmembrane signal transducer protein gp130 (CD130) and mediates the biological activities of IL-6. IL-6 binds to the membrane-bound non-signaling IL-6R alpha (mIL-6R), and the complex binds to two molecules of gp130 and leads to ‘classical’ IL-6-signal transduction, which includes activation of JAK/STAT, ERK, and PI3K signal transduction pathways (Scheller et al.). In contrast, a soluble form of IL-6R alpha (sIL-6R), which comprises the extracellular portion of the receptor, binds to the secreted IL-6 to form a complex that promotes bioavailability of IL-6. The complex of IL-6 and sIL-6R can bind to gp130 on cells that do not express the IL-6R and are unresponsive to IL-6. This process is known as trans-signaling (Hunter and Jones; Rose-John S). sIL-6R regulates both local and systemic IL-6-mediated events. Elevated levels of sIL-6R have been documented in several disease conditions such as rheumatoid arthritis, myeloma, and Crohn’s disease (Jones et al.; Mihara et al.).

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R-Spondin-1 (RSPO1) is the prototype member of the R-Spondin (RSPO) protein subfamily of a superfamily of thrombospondin type 1 repeat (TSR-1)-containing proteins (Chen et al.; Kamata et al.; Kazanskaya et al.; Kim et al.). Although unable to initialize signaling, RSPO family members are potent enhancers of WNT signaling (Cruciat and Niehrs; de Lau et al.; Kamata et al.; Kazanskaya et al.). They are characterized by a TSR-1 domain, a carboxy-terminal region with positively charged amino acids, and two N-terminal furin-like cysteine-rich repeats (Glinka et al.; Kazanskaya et al.). R­-Spondin-1 activates β­-catenin signaling via the WNT signaling cascade and by indirectly increasing low-density lipoprotein receptor-related protein 6 (LRP6) on the cell surface. It does this by binding leucine-rich repeat-containing G-protein-coupled receptor 5 (LGR5), and competing with WNT antagonist DKK­1 for binding to the WNT co­receptors, Kremen and LRP­6, which reduces DKK­1-­mediated internalization of LRP6 (Binnerts et al.). RSPO1 is involved in a wide range of pleiotropic roles during embryogenesis, it is required for the specification of hematopoietic stem cells, and it has been shown to be important in the growth, survival, and migration of ovarian cancer cells (Cruciat and Niehrs; de Lau et al.; Genthe and Clements; Liu et al.).

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Heregulin-beta 1 also known as neuregulin-1 (NRG-1) is a member of the epidermal growth factor (EGF) family of growth factors and acts as a ligand for ErbB family receptor tyrosine kinases (Britsch et al.). Heregulin/neuregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3, and NRG4). Heregulin-beta 1 plays an important role during the development of the nervous system, heart, and mammary glands (Britsch). Heregulin-beta 1 is expressed in neuronal cells, and modulates cell growth and differentiation of the cells during development and wound healing (Mei and Xiong). It has been implicated through in vivo and in vitro studies that heregulin-beta 1/ErbB signaling is crucial for multiple aspects of cardiovascular development and protects the heart from ischemic injury (Odiete et al.). Heregulin-beta 1 also promotes invasiveness and metastasis of breast cancer cells (Hutcheson et al.). It has also been shown that heregulin-beta 1 has a role in the growth and maintenance of human embryonic stem cells (Wang 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 was first purified from the culture of mouse lung tissue after lipopolysaccharide treatment. 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 (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.).

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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. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src, and PI3K/AKT (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.). It has been shown that PDGF-AB together with 5-Azacytidine (Catalog #72012), induces the conversion of mature bone and fat cells into tissue-regenerative multipotent stem cells (Chandrakanthan et al.).

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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 T helper type 2 (Th2) cells, which produce IL-4, IL-5, IL-10, and IL-13 (Bao et al.; Olpihant et al.; Nelms et al.). In addition to Th2 T cells, IL-4 is produced by CD4+ NK T cells, γ/δ T cells, activated basophils, eosinophils, and mast cells. IL-4 consists of 130 amino acids with a predicted molecular weight of 15.1 kDa. Human IL-4 does not cross-react with mouse cells (Park et al.). This product is animal component-free.

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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 regulatory cells, as well as mast cells, NK cells, neutrophils, and regulatory B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the activation of certain immune cells while it promotes the function of B cells, and facilitate healing process. Specifically, this cytokine is important for the function of T regulatory cells as it is a potent suppressor of effector T cell proliferation and cytokine production. Also, IL-10 produced by a subset of macrophages inhibits activation and production of pro-inflammatory cytokines by neighboring macrophages, thus allowing a level of self-regulation. IL-10 enhances B cell proliferation, immunoglobulin secretion, and class II MHC expression (Ouyang et al.).

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Tumor necrosis factor-alpha (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 cancerous cells 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 and Hošek). Other effects of TNF-α include vasodilatation and edema formation. In vitro studies of adult rat neural progenitor cells (NPCs) demonstrate that TNF-α reduces neurogenesis in dentate gyrus-derived NPCs, and promotes astrogliogenesis in subventricular zone-derived NPCs (Borsini et al.).

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RANTES (regulated upon activation, normal T cell expressed and secreted), also known as CCL5, is a member of the CC family of chemokines and is able to recruit leukocytes to sites of inflammation (Schall et al.). RANTES is secreted by T lymphocytes, macrophages, platelets, synovial fibroblasts, tubular epithelium, and certain types of tumor cells (Aldinucci and Colombatti; Soria and Ben-Baruch). This chemokine exerts its effect by interacting with the chemokine receptors CCR1, CCR3, CCR4, and CCR5. RANTES plays an active role in recruiting a variety of leukocytes into inflammatory sites, including T cells, macrophages, eosinophils, and basophils. In collaboration with certain cytokines that are released by T cells such as IL-2 and IFN-γ, RANTES also induces the activation and proliferation of NK cells to generate CC chemokine-activated killer cells, which are highly cytolytic (Lv et al.; Maghazachi et al.). It has been shown that RANTES produced by CD8+ T cells inhibits HIV infection of primary human peripheral blood mononuclear cells (Appay and Rowland-Jones; Cocchi et al.).

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Interleukin 13 (IL-13) is a cytokine important in type 2 immune responses and is expressed by T helper type 2 (Th2) cells and group 2 innate lymphoid cells (ILC2s) (Pulendran and Artis). IL-13 binds a receptor composed of IL-4Ra and IL-13Ra1 or IL-13Ra2 (Wynn 2003). IL-13 receptor is expressed on B cells and promotes B cell proliferation, induces class switching to IgG4 and IgE, and functions in the recruitment and activation of IgE-producing B cells (Hershey). The receptor is also expressed on basophils, eosinophils, mast cells, endothelial cells, fibroblasts, monocytes, macrophages, respiratory epithelial cells, and smooth muscle cells (Hershey). Signaling through the IL-13 receptor activates the JAK/STAT and IRS-1/IRS-2 pathways. in vivo, IL-13 has a role in resistance to extracellular helminth parasites by regulating gastrointestinal parasite expulsion, as well as in airway hyperresponsiveness, allergic inflammation, tissue remodeling, tumor cell growth, and fibrosis (Wynn 2015). Secreted IL-13 is a protein consisting of 112 amino acids with a molecular mass of 10 kDa (Hershey). Human IL-13 is not species-specific but has greater activity on human cells compared to mouse cells (Hershey).

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Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to the LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells; however, mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.).

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The platelet-derived growth factor (PDGF) family has five heparin-binding members that assemble into four homodimers (PDGF-AA, PDGF-BB, PDGF-CC, and PDGF-DD) and one heterodimer (PDGF-AB; Fretto et al.; Li and Eriksson). PDGF signals through the receptor tyrosine kinases PDGFRα and PDGFRβ. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src, and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin, such as 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-DD promotes growth and survival of renal artery smooth muscle cells and lens epithelial cells, and can act as a macrophage chemoattractant (Changsirikulchai et al.; Lokker et al.; Ray et al.; Uutela et al.).

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Neurotrophin-3 (NT-3) is a neurotrophic factor and a member of the nerve growth factor (NGF) family of proteins that includes neuron growth factor (NGF), brain-derived neurotrophic factor (BDNF), and neurotrophin-4/5. NT-3 signals a number of trophic effects through its transducing receptor tyrosine kinase TrkC. NT-3 is known to promote survival, development, and differentiation of neurons, and modulates transmitter release at several types of synapses in the peripheral and central nervous systems (Chalazonitis 1996). NT-3 has been shown to have an important role in the overall development of enteric neurons, which are crucial for gut peristalsis (Chalazonitis 2004). Studies in rats have shown the potential of NT-3 in dorsal column axonal regeneration (Bradbury et al.). NT-3 was shown to protect neurons against amyloid-β toxicity (Lesne et al.). NT-3 has applications in neuronal differentiation protocols to generate β-tubulin III+ peripheral neurons from neural crest stem cells (Menendez et al.) and oligodendrocyte precursor cells from human embryonic stem (ES) and induced pluripotent stem (iPS) cells (Douvaras 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 heterodimers of the IL-21 receptor (IL-21R) and the IL2RG encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (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 NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki 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 heterodimers of the IL-21 receptor (IL-21R) and the IL2RG-encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (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 NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.). This product is animal component-free.

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Oncostatin M (OSM) is a member of interleukin 6 (IL-6) family of cytokines and bears close resemblance to leukemia inhibitory factor (LIF) and granulocyte colony-stimulating factor (G-CSF) in amino acid sequence and its modulation of differentiation in a variety of cell types (Rose and Bruce). OSM signals through type I receptor (consisting of gp130 and LIF receptor [LIFR]) and type II receptor (consisting of gp130 and OSM receptor [OSMR]), which eventually activate the JAK/STAT pathway (Auguste et al.; Gómez-Lechón). OSM is primarily produced by activated T cells and monocytes, and also by activated macrophages, neutrophils, mast cells, and dendritic cells. OSM is also produced within the bone microenvironment by cells of both hematopoietic and mesenchymal origin, including osteocytes and osteoblasts. OSM is involved in differentiation, cell proliferation, hematopoiesis, and inflammation, and also has been shown to have implications in liver development and bone formation and resorption (Sims and Quinn; Tanaka and Miyajima). This product is animal component-free.