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Galectin-1 (Gal1) was the first characterized member of the galectin family of galactosidase-binding proteins, with over 15 mammalian galectins identified (Camby et al.; Salatino et al.). Gal1 comes in two forms: the oxidized monomer that acts as a cytokine, and the reduced dimer that acts as a lectin (Gaudet et al.). This product is in the dimer form. This cytokine is expressed in many tissues and has an immunosuppressive role in affecting T cell homeostasis by various mechanisms such as regulating apoptosis, cytokine secretion, cell adhesion, cell proliferation, and other effects (Camby et al.; Garín et al.; Gaudet et al.; Salatino et al.). In addition, Gal1 is thought to also play a role in axonal regeneration after injuries (Camby et al.; Garín et al.; Gaudet et al.; Salatino et al.). There are several therapeutic applications suggested for Gal1; overexpression has been suggested as a therapy for autoimmune and inflammatory diseases and enhancing axonal regeneration in injured nerves (Camby et al.; Gaudet et al.). In contrast, inhibition of Gal1 has been suggested to prevent tumor metastasis and cancer progression, as it may aid in cell adhesion, migration, and immune escape of cancer cells (Camby et al.).

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Leptin is a protein produced from the ob gene or lep gene, and acts as both a hormone involved in metabolic function as well as a proinflammatory cytokine by inducing Th1 immune responses (Dunn et al.; La Cava; Newman and Gonzalez-Perez). Leptin is a member of the gp130 family of cytokines and is known to be correlated with obesity (Dixit et al.; Dunn et al.). Leptin can both promote osteogenesis via osteoblast receptors and inhibit it through its actions on the hypothalamus (Figenschau et al.). It is a small, non-glycosylated protein with a highly conserved sequence between species. Leptin binds to the leptin receptor OB-R, which exists in six isoforms in humans and can activate various Janus kinase (JAK) and downstream pathways (Dunn et al.; Münzberg and Morrison; Newman and Gonzalez-Perez). For example, the binding of leptin to LepRb receptor activates JAK2, which leads to the phosphorylation of both JAK2 and the LepRb receptor, with three separate residues on the receptor triggering signaling pathways for SHP-2, STAT5, and STAT3 (Dunn et al.; Münzberg and Morrison). In addition to its effects on mature immune cells, other studies have suggested impacts on other cell types, with activities such as inducing cell proliferation and morphological differentiation in hematopoietic cell lines, chondrocytes, and hepatic cells (Figenschau et al.; Gainsford et al.; Santos-Alvarez et al.; Wang et al.).

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A cytokine belonging to the type 1 interferon family, Interferon beta (IFN beta) binds IFN alpha/beta receptors (IFNAR) that activate tyrosine kinases and initiate the interferon-induced Jak-STAT signaling pathway, which modulates many key immune processes (Smieja et al.). In an experimental model involving cardiac fibroblasts isolated from rats, IFN beta was found to induce both pro- and anti-inflammatory cytokines production by activating different STAT proteins (Bolivar et al.). The anti-inflammatory effects of IFN beta have been studied in the context of autoimmune disorders, and there are currently multiple approved IFN beta drugs for treatment of relapsing forms of multiple sclerosis (Filipi and Jack). IFN beta is produced by immune cells, including macrophages, and non-immune cells, such as fibroblasts and epithelial cells (Ivashkiv and Donalin). The crystal structure of IFN beta shares characteristics with other type I interferons. It comprises five alpha-helices with four of them forming a helix bundle, and one long and three shorter loops connecting the helices (Karpusas et al.). For consistency and reproducibility across your applications, interferon alpha 1 from STEMCELL comes lyophilised with ≥87% purity, specific activity EC50 ≤18 pg/mL, and LAL analysis verification ensuring endotoxin levels are ≤1,0 EU/μg protein.

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Interleukin 6 (IL-6) is a pleiotropic growth factor with the wide range of biological activities in immune regulation, hematopoiesis, and oncogenesis. IL-6 is produced by a variety of cell types including T cells, B cells, monocytes and macrophages, fibroblasts, hepatocytes, vascular endothelial cells, and various tumor cell lines. On its own or in combination with other factors such as IL-2 and interferon-γ, IL-6 stimulates the proliferation of B cells, T cells, and hybridoma cells (Hirano et al.; Mihara et al.; Tanaka et al). In combination with cytokines such as IL-3, GM-CSF and SCF, IL-6 has been shown to promote hematopoietic progenitor cell proliferation and differentiation in vitro. IL-6 signals through a cell surface type I cytokine receptor complex consisting of the ligand-binding IL-6α (CD126) and the signal-transducing gp130 subunits. The binding of IL-6 to its receptor system includes activation of JAK/STAT signaling pathway (Mihara et al.; Peters et al.; Tanaka et al.). This product is animal component-free.

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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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Fibroblast growth factor 8B (FGF-8B) is a member of the fibroblast growth factor (FGF) family and is an isoform of FGF-8. Cytokines in the FGF family possess broad mitogenic and cell survival activities (Folkman andamp; Klagsbrun; Kimelman andamp; Kirschner) and are involved in a variety of biological processes, including cell proliferation, differentiation, survival, and apoptosis (Folkman andamp; Klagsbrun; Klagsbrun; Rifkin andamp; Moscatelli). FGF-8B signals through FGF receptors (FGFRs) to activate PI3K and MAPK pathways. FGF-8B is broadly associated with mitogenic and cell survival activities, and regulates gastrulation, epithelial-mesenchymal transition, and later on mesenchymal to epithelial differentiation during embryonic development. FGF-8B has also been found in peripheral blood leukocytes and healthy bone marrow samples (Mattila andamp; Härkönen). FGF-8B has mitogenic effects on somatic cells in the germinal epithelium and is expressed in adult mouse ovarian cells and tissues, which suggests that it regulates maturation of oocytes and seminiferous epithelium in testis (Valve et al.).

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A type 1 membrane glycoprotein belonging to the immunoglobulin superfamily, cluster of differentiation 200 (CD200) binds the CD200 receptor (CD200R) that is expressed on the surface of myeloid cells and T cells (Wright et al.), and has been shown to inhibit myeloid cell activity and macrophage cytokine production (Jenmalm et al.). Homologues of CD200 have been identified in viruses and can interact with CD200R to reduce macrophage pro-inflammatory cytokine production (Foster-Cuevas et al.). Studies have shown that the immunosuppressive effects of CD200 can promote acceptance of allogeneic tissue grafts in hosts (Gorczynski et al.), whereas dysregulation of CD200/CD200R can contribute to the development of autoimmune conditions, such as rheumatoid arthritis (Ren et al.). CD200 contains two immunoglobulin-like domains, a V-type domain and a smaller C2-type domain (Hatherley et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, cluster of differentiation 200 from STEMCELL comes lyophilised with ≥95% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein. Human recombinant CD200 at 2 μg/ml can bind human CD200R (His and hFc tag) with a linear range of 5 to 28 ng/ml, as determined by functional ELISA.

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Stromal cell-derived factor 1 alpha (SDF-1α) is a member of the CXC group of chemokines that binds to the G-protein coupled receptor, CXCR4, to regulate migration, proliferation, differentiation, and survival of many cell types including hematopoietic stem cells, B cells, and T cells. It is produced by bone marrow stromal cells, osteoblasts, endothelial cells, and neuronal cells. SDF-1α was first identified as the pre-B-cell growth-stimulating factor (PBSF) in the mouse bone marrow-derived stromal cell line, PA6, in the growth of B cell precursors (Hayashi et al.). SDF-1α primarily regulates cell motility during development and adulthood, including the homing of hematopoietic stem cells and neutrophils to fetal bone marrow during ontogeny (Ara et al. 2003a) and the recruitment of endothelial progenitor cells from bone marrow during angiogenesis in adulthood (Zheng et al.). In addition to its role in hematopoiesis, the SDF-1α/CXCR4 signaling pathway is also essential for the homing of primordial germ cells to gonads (Ara et al. 2003b), the migration of granule cells in the cerebellum during neurogenesis (Zou et al.), and the migration of breast cancer cells to sites of metastasis (Muller et al.).

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Midkine is a member of a unique family of heparin-binding growth factors that are structurally different from other fibroblast growth factors (Muramatsu; Takada et al.). Midkine is a proinflammatory cytokine, promoting the migration of leukocytes, fibrinolysis, and acting as a chemotactic agent towards neutrophils (Muramatsu; Said et al.; Takada et al.). It also regulates growth, differentiation, and development during the midgestion stage of embryogenesis, and promotes angiogenesis (Muramatsu; Said et al.; Takada et al.). The protein structure consists of three antiparallel β-sheets and is highly conserved between species (Muramatsu; Takada et al.). While the exact signal pathway is not known, proposed pathways include promoting LRP, inhibiting Src kinase, activating paxillin and STAT1α, activating PI2 and MAP kinases, suppressing caspases, binding to α6β1-integrin and tetraspanin, activating FAK, phosphorylating STAT3, suppressing STAT5 phosphorylation, activating ALK, activating PI3 kinase and transcription of NFkB, binding to neuroglycan C or nucleolin, and binding to eIF3 (Muramatsu). In cultured cells, midkine influences growth and survival of neural precursor cells, synthesis of cytokines from endothelial and renal epithelial cells, and promotes synthesis of extracellular matrices from fibroblasts (Muramatsu; Takada 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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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.). 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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Betacellulin is a member of the epidermal growth factor (EGF) family, and signals through EGF receptor and ERBB4. It activates ERK and AKT pathways, which induces neural stem cell proliferation and prevents spontaneous differentiation in culture. Betacellulin stimulates the expansion of neural stem cells, transit-amplifying cells, and neuroblasts derived from subventricular zone and dentate gyrus (Gómez-Gaviro et al.). It is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Betacellulin down-regulates E-cadherin expression in ovarian cancer cell lines via MEK/ERK1/2 and PI3K/AKT signaling pathways, thus increasing cell migration (Zhao et al.). It is a modulator of interferon (IFN) response and enhances anti-viral effects of IFN (Al-Yahya et al.). Betacellulin is expressed in pancreatic α cells, β cells, and duct cells. It induces the proliferation of pancreatic cancer cell lines, inhibits apoptosis, promotes the neogenesis of β cells, and converts non-β cells into insulin-producing cells (Kawaguchi et al.; Miyagawa al.; Saito 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.

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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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Use Interferon beta (IFN-β) to modulate the activity of genes that control dendritic cell activation, T cell survival, NK cell activation, chemokine expression, lymph node retention, and antiproliferative and antiviral effects (Dunn et al. Nat Rev Immunol, 2006). IFN-β binds to a receptor complex composed of IFNAR1 and IFNAR2, and initiates signal transduction via the JAK/STAT pathway. It is predominantly produced by fibroblasts, with smaller amounts from plasmocytoid dendritic cells. Macrophages and endothelial cells secrete IFN-β in response to viral infection (Reder and Feng. Front Immunol, 2013). IFN-β suppresses Th17 cells by affecting expression of IL-4, IL-10, and IL-27, and is a first-line treatment for multiple sclerosis. IFN-β was also shown to expand regulatory T cells and limit T cell trafficking to the central nervous system (Inoue and Shinohara. Immunology, 2013). Of the two IFN-β variants (IFN-β1 and IFN-β3), this product is the IFN-β1 form.

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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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Interleukin 6 (IL-6) is a pleiotropic growth factor with the wide range of biological activities in immune regulation, hematopoiesis, and oncogenesis. IL-6 is produced by a variety of cell types including T cells, B cells, monocytes and macrophages, fibroblasts, hepatocytes, vascular endothelial cells, and various tumor cell lines. On its own or in combination with other factors such as IL-2 and interferon-γ, IL-6 stimulates the proliferation of B cells, T cells, and hybridoma cells (Hirano et al.; Mihara et al.; Tanaka et al). In combination with cytokines such as IL-3, GM-CSF and SCF, IL-6 has been shown to promote hematopoietic progenitor cell proliferation and differentiation in vitro. IL-6 signals through a cell surface type I cytokine receptor complex consisting of the ligand-binding IL-6α (CD126) and the signal-transducing gp130 subunits. The binding of IL-6 to its receptor system includes activation of JAK/STAT signaling pathway (Mihara et al.; Peters et al.; Tanaka et al.).

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Interleukin 15 (IL-15) is a four-alpha helix bundle cytokine with many similar properties to IL-2, with which it shares components of its receptor. The IL-15 receptor is a heterotrimeric receptor composed of IL-15Ra, the high-affinity receptor for IL-15, as well as IL-2/15Rb (CD122) and common gamma chain (CD132). IL-15 binds to IL-15Rα receptor and can then be presented in trans to IL-2/15Rb and common gamma chain on other cells. Trans-presentation is thought to be the major mechanism by which IL-15-mediated responses occur in mice, although may not be necessary in humans (Castillo et al.). The cytoplasmic domains of IL-2/15Rb and common gamma chain mediate signaling to activate JAK/STAT and PI3K pathways. IL-15 supports the survival and proliferation of naive CD4+ and CD8+ T cells, and promotes homeostasis of memory T cells. IL-15 also promotes the survival and differentiation of NK cells and regulates their cytolytic activity (Ma 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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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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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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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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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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Use autotaxin (ENPP2) to catalyse the production of lysophosphatidic acid (LPA), a potent mitogen that can evoke growth factor-like responses (Moolenaar and Corven), from lysophospholipids in extracellular fluids. Autotaxin is a secreted glycoprotein that belongs to the ectonucleotide pyrophosphatase/phosphodiesterase (ENPP) family, containing two N-terminal somatomedin B (SMB)-like domains, a central phosphodiesterase (PDE) domain with an active catalytic site, and a C-terminal nuclease-like (NUC) domain (Nishimasu et al.). Dysregulation of autotaxin and LPA receptors is implicated in cancer (Tigyi et al.), fibrosis (Ninou et al.), neurological disorders (Roy et al.), and other inflammation-associated conditions. Both Autotaxin and LPA are overexpressed in many cancers and can promote cell proliferation, migration, and resistance to apoptotic death (Tigyi et al.). Autotaxin was also found to catalyse the production of cyclic phosphatidic acid (CPA), an analog of LPA, which has anti-mitogenic and inhibitory effects on tumor cell invasion and metastasis (Fujiwara). This protein contains a His-residue tag at the amino end of the polypeptide chain. For consistency and reproducibility across your applications, Autotaxin from STEMCELL comes lyophilised with ≥85% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.