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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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Brain-derived neurotrophic factor (BDNF), like nerve growth factor (NGF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4), is a member of the NGF family of neurotrophins, which are required for the differentiation and survival of specific neuronal subpopulations in both the central and the peripheral nervous systems (Minichiello and Klein; Minichiello et al.). BDNF binds with high affinity to the TRKB kinase receptor, and activates AKT and ERK pathways (Mattson et al.). It is expressed in hippocampus, cortex, and synapses of the basal forebrain. BDNF acts as a survival factor for human embryonic stem cells when plated on either feeder cells or Corning® Matrigel® (Pyle et al.). BDNF regulates synaptic transmission and plasticity at adult synapses in the central nervous system, contributes to adaptive neuronal responses including long-term potentiation, long-term depression, certain forms of short-term synaptic plasticity, as well as homeostatic regulation of neuronal excitability (Reichardt). It also has a role in neurogenesis by promoting survival and growth of dorsal root ganglion cells, and hippocampal and cortical neurons (Binder and Scharfman). BDNF, together with glial cell-derived neurotrophic factor (GDNF) and other supplements, is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Brafman). This product is animal component-free.

Supplier: STEMCELL Technologies

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.

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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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Macrophage inflammatory protein-1 beta (MIP-1 beta), also known as CCL4, is a member of the CC family of chemokines and is most closely related to CCL3 (MIP-1 alpha). Cellular sources of MIP-1 beta include activated leukocytes (monocytes and T and B cells), brain endothelial cells, and smooth muscle cells (Lukacs et al.; Menten et al.). MIP-1 beta, MIP-1 alpha, and RANTES have been shown to be major HIV-suppressive factors, possibly through the interactions of these chemokines with the receptor CCR5 on CD4+ T cells, which is also a major receptor for HIV entry into CD4+ T cells (Cocchi et al.; Menten et al.). MIP-1 beta attracts a variety of immune cells to sites of microbial infection. In addition to its chemotactic functions, MIP-1 beta induces the release of proinflammatory cytokines, mast cell degranulation, and NK cell activation (Schall et al.). In mice, recruitment of regulatory T cells to B cells and antigen-presenting cells by MIP-1 beta plays a central role in the initiation of T cell and humoral responses, and the depletion of regulatory T cells or MIP-1 beta results in deregulated humoral responses and production of autoantibodies (Bystry et al.).

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Macrophage colony-stimulating factor (M-CSF) is a homodimeric glycoprotein growth factor that regulates proliferation and differentiation of myeloid hematopoietic progenitors to mononuclear phagocytic cell lineages, including monocytes, macrophages, and osteoclasts. M-CSF is a crucial factor for the development of tissue-resident macrophages in most tissues (Ginhoux andamp; Jung). It is required for the maturation and activation of monocytes and macrophages, and regulates inflammatory responses in conjunction with other stimuli such as IFN-γ, LPS, and IL-4 (Murray et al.). M-CSF is also required for bone resorption by osteoclasts, and is involved in the development and regulation of placenta, mammary gland, and brain. M-CSF is produced by monocytes, fibroblasts, osteoclasts, stromal cells, endothelial cells, and tumor cells (Chockalingam andamp; Ghosh). M-CSF exerts its biological effects by signaling through a receptor tyrosine kinase (CSF-1R or M-CSF-R) encoded by the c-fms proto-oncogene (Hamilton). CSF-1R shares similar structural features with other growth factor receptors, including the stem cell factor (SCF) receptor, platelet-derived growth factor receptor (PDGF-R), and Flt3/Flk-2 receptor tyrosine kinase. Stimulation of the CSF-1R upon binding to M-CSF activates MAPK, PI3K, and PLCγ signaling pathways (Chockalingam andamp; Ghosh). Human and mouse M-CSF sequences are highly conserved both at nucleotide and amino acid levels (80% homology; DeLamarter et al.). This product is animal component-free.

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Trigger a variety of immunological responses with E. coli Lipopolysaccharide O55:B5 (S-form), a lipopolysaccharide (LPS) derived from the O55:B5 serotype of the Gram-negative bacteria and nbsp Escherichia coli. Composed of a lipid A, a core oligosaccharide, and an O antigen, LPS are glycolipid constituents that reside on the outer membranes of gram-negative bacteria (Kitchens RL et al.). LPS protects bacteria against bile salts and lipophilic antibiotics by maintaining the outer integrity of the cell membrane (Bäckhed F et al.). E. coli lipopolysaccharide O55:B5 (S-form), in particular, is predominantly recognized by toll-like receptor 4 (TLR4), which leads to the activation of NF-κβ, a protein complex which plays a key role in regulating immune response (Kuzmich N et al.). Activation of NF-κβ can trigger increased production of pro-inflammatory cytokines IL-1 and TNF-α by macrophages (Matuschak GM et al.). This LPS can also interact with CD14 to activate phospholipase Cγ2 and kinases of the Src family, trigger influxes of extracellular Ca2+, as well as calcineurin-dependent translocation of the nuclear factor of activated T cells (NFAT) family of transcription factors (Li CC et al.). When added to ImmunoCult™-SF macrophage medium (Catalog #10961), stimulation with lipopolysaccharide from E. coli (O55:B5) and IFN-γ supports the polarization to M1 (classically activated) macrophages. Warning: This product is highly pyrogenic. Avoid all means by which the product may enter the bloodstream.

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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, complement, etc. (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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Fibroblast growth factor 10 (FGF-10) is a member of the fibroblast growth factor (FGF) family which is 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) and endodermal differentiation of human pluripotent stem cells to insulin-producing pancreatic-like cells (Takeuchi et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

Brain-derived neurotrophic factor (BDNF), like nerve growth factor (NGF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4), is a member of the NGF family of neurotrophins, which are required for the differentiation and survival of specific neuronal subpopulations in both the central and the peripheral nervous systems (Minichiello and Klein; Minichiello et al.). BDNF binds with high affinity to the tropomyosin receptor kinase B (TrkB), and activates AKT and ERK pathways (Mattson et al.). It is expressed in the hippocampus, cortex, and synapses of the basal forebrain. BDNF acts as a survival factor for human embryonic stem cells when plated on either feeder cells or Corning® Matrigel® (Pyle et al.). BDNF regulates synaptic transmission and plasticity at adult synapses in the central nervous system, and contributes to adaptive neuronal responses including long-term potentiation, long-term depression, certain forms of short-term synaptic plasticity, and homeostatic regulation of neuronal excitability (Reichardt). It also has a role in neurogenesis by promoting survival and growth of dorsal root ganglion cells, and hippocampal and cortical neurons (Binder and Scharfman). BDNF, together with glial cell line-derived neurotrophic factor (GDNF) and other supplements, is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Brafman).

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Interleukin 34 (IL-34) is well known for its ability to induce the formation of colony-forming unit macrophages in human bone marrow cell cultures (Foucher et al.; Wei et al.). This dimeric glycoprotein is a member of the short-chain helical hematopoietic cytokine family (Baghdadi et al.; Foucher et al.), and exists in two isoforms that differ by a single glutamine (Chen et al.; Foucher et al; Wei et al.). IL-34 interacts with M-CSF to trigger tyrosine phosphorylation of the receptor and ERK1/2 pathways. (Wang et al.; Wei et al.). It is expressed in many tissues (heart, brain, lung, liver, kidney, thymus, testes, ovary, small intestine, prostate, and colon), with the highest expression in the spleen. In combination with RANKL, IL-34 induces osteoclast differentiation (Chen et al.; Foucher et al.). IL-34 expression is decreased in Alzheimer’s disease and atopic dermatitis, while high levels of IL-34 are found in many types of cancer correlated with poor prognosis, chronic heart failure or coronary artery disease, inflammatory bowel disease, influenza A infection, during acute liver transplant rejection or in non-alcoholic fatty liver disease, and with rheumatoid arthritis (Baghdadi et al.). It is therefore a possible pharmacological target for treating bone or inflammatory diseases (Chen et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain, and the protein was purified as a homodimer consisting of 39 kDa monomers (Lin 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; 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 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-CC is secreted as a latent growth factor and requires activation by proteolytic processing (Li and Eriksson). PDGF-CC binds to PDGFRα homodimers and PDGFRαβ heterodimers, but not to PDGFRβ homodimers (Li and Eriksson). PDGF-CC is an angiogenic factor that stimulates coronary artery smooth muscle cell proliferation and plays a role in cardiovascular development (Gilbertson et al.). PDGF-CC is also expressed in many tumors and plays a role in tumorigenesis (Zwerner and May).

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Ciliary neurotrophic factor (CNTF) is a neurotrophic factor that belongs to the four-helix bundle cytokine family and is structurally related to interleukin 6 (IL-6), interleukin 11 (IL-11), leukemia inhibitory factor (LIF), and oncostatin M (OSM). CNTF binds to its receptor CNFTRα and induces formation of a heterodimer of the signal-transducing IL-6 receptor gp130 and LIF receptor (LIFR)-β, which triggers JAK/STAT, ERK, and the PI3K signaling cascades (Schuster et al.). CNTF plays an important role in neurogenesis and the differentiation of neural stem cells and has been suggested to possess a therapeutic role in treating neurological disorders (Ding et al.; Oppenheim et al.). CNTF has also been shown to protect rod photoreceptors from light-induced damage and to have therapeutic effects on retinal degenerative diseases caused by genetic defect or damage induced by toxins, autoantibodies, or strong light (Pernet et al.; Rhee et al.). Another therapeutic role of CNTF has been reported in protecting oligodendrocytes from death induced by apoptosis (Louis et al.). Additionally, CNTF is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into astrocytes (Krencik and Zhang).

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Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor and a member of the tumor growth factor (TGF)-beta superfamily. The GDNF family of growth factors also includes neurturin, persephin, and artemin, which have seven conserved cysteine residues called cysteine-knots (Treanor et al.). GDNF family ligands signal through binding to specific GDNF-family receptor-α (GFRα) co-receptors and activate the RET receptor tyrosine kinase (Durbec et al.). Four different forms of GFRα co-receptors have been characterized (GFRα 1-4); GDNF binds specifically to GFRα1 prior to forming a complex with RET (Airaksinen and Saarma). GDNF is known to promote survival and morphological differentiation of midbrain dopaminergic neurons in both in vivo and in vitro studies and increases their high-affinity dopamine uptake (Granholm et al.; Lin et al.). GDNF has also been shown to have restorative effects on dying dopaminergic neurons in response to degenerative toxins (Aoi et al.). GDNF, together with Human Recombinant BDNF (brain-derived neurotrophic factor), BrainPhys™ Neuronal Medium, and other supplements, can be used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Bardy et al.).

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Vascular endothelial growth factor (VEGF) is a heparin-binding homodimeric glycoprotein involved in vasculogenesis and angiogenesis. VEGF binds to FLT1 (VEGFR-1) and KDR (VEGFR-2), and activates Raf/MEK/ERK and PI3K/AKT pathways (Ferrara et al.). VEGF exists in multiple isoforms that result from alternative splicing of VEGF mRNA in the terminal exon. Proximal splice-site selection in exon 8 results in pro-angiogenic VEGFxxx isoforms (xxx is the number of amino acids), whereas distal splice-site selection results in anti-angiogenic VEGFxxxb isoforms (Nowak et al.). VEGF plays an important role in neurogenesis both in vitro and in vivo (Storkebaum et al.). It has neurotrophic effects on neurons of the central nervous system, and it promotes growth and survival of dopaminergic neurons and astrocytes. VEGF also promotes growth and survival of vascular endothelial cells, monocyte chemotaxis, and colony formation by granulocyte-macrophage progenitor cells (Ferrara et al.). Various splice variants of VEGF exist, with different functions. For example, it has been shown that VEGF isoform VEGF-164(165) and not VEGF-120(121) induces inflammation, stimulates intracellular adhesion molecule (ICAM)-1 expression on endothelial cells, and induces chemotaxis of monocytes (Usui et al.).

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Stem cell factor (SCF) is an early-acting cytokine that plays a pivotal role in the regulation of embryonic and adult hematopoiesis. SCF promotes cell survival, proliferation, differentiation, adhesion, and functional activation of cells at multiple levels of the hematopoietic hierarchy. Together with other cytokines such as thrombopoietin and Flt3/Flk-2 Ligand, SCF is commonly used to promote expansion of primitive hematopoietic stem cells and multi-potent progenitor cells in culture (Martin et al.; Kent et al.). In synergy with various growth factors, including IL-2, IL-3, IL-6, IL-7, G-CSF, and erythropoietin, SCF increases proliferation and differentiation of myeloid and erythroid progenitor cells and a subset of lymphoid progenitor cells (Broudy). SCF is also a primary growth and activation factor for mast cells and eosinophils. SCF exists in two biologically active splice forms: a soluble and a transmembrane isoform. Upon binding to its receptor (c-Kit tyrosine kinase receptor; CD117), it activates PI3K, JAK/STAT, and MAPK pathways. SCF and signaling from c-Kit have also been reported to play an important role in pigmentation, fertility, vasculogenesis, motility of the gut via c-Kit positive interstitial cells of Cajal, and in the migration of neuronal stem and progenitor cells to sites of injury in the brain. This product is animal component-free.

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Macrophage colony-stimulating factor (M-CSF) is a homodimeric glycoprotein growth factor that regulates proliferation and differentiation of myeloid hematopoietic progenitors to mononuclear phagocytic cell lineages, including monocytes, macrophages, and osteoclasts. M-CSF is a crucial factor for the development of tissue-resident macrophages in most tissues (Ginhoux andamp; Jung). It is required for the maturation and activation of monocytes and macrophages, and regulates inflammatory responses in conjunction with other stimuli such as IFN-γ, LPS, and IL-4 (Murray et al.). M-CSF is also required for bone resorption by osteoclasts, and is involved in the development and regulation of placenta, mammary gland, and brain. M-CSF is produced by monocytes, fibroblasts, osteoclasts, stromal cells, endothelial cells, and tumor cells (Chockalingam andamp; Ghosh). M-CSF exerts its biological effects by signaling through a receptor tyrosine kinase (CSF-1R or M-CSF-R) encoded by the c-fms proto-oncogene (Hamilton). CSF-1R shares similar structural features with other growth factor receptors, including the stem cell factor (SCF) receptor, platelet-derived growth factor receptor (PDGF-R), and Flt3/Flk-2 receptor tyrosine kinase. Stimulation of the CSF-1R upon binding to M-CSF activates MAPK, PI3K, and PLCγ signaling pathways (Chockalingam andamp; Ghosh). Human and mouse M-CSF sequences are highly conserved both at nucleotide and amino acid levels (80% homology; DeLamarter 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 progenitors (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 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. Recombinant human GM-CSF (rhGM-CSF) promotes the production of myeloid cells of the granulocytic (neutrophils, eosinophils and basophils) and monocytic lineages in vivo. It has been tested for mobilisation of hematopoietic progenitor cells and for treating chemotherapy-induced neutropenia in patients. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.). This product is animal component-free.

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Interleukin-8 (IL-8) is a member of the CXC subfamily of chemokines and is produced by leukocytic cells (monocytes, T cells, neutrophils, and natural killer cells) and non-leukocytic somatic cells (endothelial cells, fibroblasts, and epithelial cells), with the most prominent source being monocytes and macrophages. Its production is induced by inflammatory stimuli, such as IL-1. IL-8, also known as CXCL8, activates neutrophils inducing chemotaxis, exocytosis, and the respiratory burst (Baggiolini and Clark-Lewis; Mukaida). IL-8 is considered one of the most potent neutrophil chemoattractants in inflammation and binds to two different chemokine receptors on leukocytes: the G protein-coupled receptors CXCR1 and CXCR2 (Hoffmann et al.; de Oliveira et al.). IL-8 has angiogenic effects on human intestinal microvascular endothelial cells in vitro that are mediated by CXCR2 (Heidemann et al.). IL-8 is reported to promote breast cancer progression by increasing cell invasion, angiogenesis, and metastasis and has been reported to be involved in regulating breast cancer stem-like cells (Singh et al.). IL-8 also has proangiogenic properties in inflammatory diseases of the conjunctiva, cornea, iris, retina, and orbit (Ghasemi et al.). It was also shown that a major T cell effector function in human newborns is IL-8 production, which has the potential to activate antimicrobial neutrophils and gamma/delta T cells (Gibbons et al.). A variety of human pathogens, such as HIV and Mycobacterium tuberculosis, have been shown to induce IL-8 production by monocytes and macrophages (Friedland et al.; Meddows-Taylor 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 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. Recombinant human GM-CSF (rhGM-CSF) promotes the production of myeloid cells of the granulocytic (neutrophils, eosinophils, and basophils) and monocytic lineages in vivo. It has been tested for mobilisation of hematopoietic progenitor cells and used to treat chemotherapy-induced neutropenia in patients. 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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Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor and a member of the tumor growth factor (TGF)-beta superfamily. The GDNF family of growth factors also includes neurturin, persephin, and artemin, which have seven conserved cysteine residues called cysteine-knot (Treanor et al.). GDNF family ligands signal through binding to specific GDNF-family receptor-α (GFRα) co-receptors and activate the RET receptor tyrosine kinase (Durbec et al.). Four different forms of GFRα co-receptors have been characterized (GFRα 1-4) out of which GDNF binds specifically to GFRα1 prior to forming a complex with RET (Airaksinen and Saarma). GDNF is known to promote survival and morphological differentiation of midbrain dopaminergic neurons in both in vivo and in vitro studies and increase their high-affinity dopamine uptake (Granholm et al.; Lin et al.). GDNF has also been shown to have restorative effects on dying dopaminergic neurons in response to degenerative toxins (Aoi et al.). GDNF, together with Human Recombinant BDNF (brain-derived neurotrophic factor; Catalog #78005), BrainPhys™ Neuronal Medium (Catalog #05790), and other supplements, can be used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Bardy et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

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 mobilization 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. Mouse G-CSF was first purified from cultures of the WEHI-3B myelomonocytic leukemia cell line as the inducer of the terminal differentiation of WEHI-3B and other myeloid leukemia cell lines (Nicola et al.). It was later cloned in monkey COS cells from a cDNA library prepared with mRNA derived from mouse fibrosarcoma NFSA cells that produce G-CSF constitutively (Tsuchiya et al.). 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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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, 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.). It has been suggested that PDGF-AA is an important autocrine regulator of vascular endothelial growth factor (VEGF) expression in non-small cell lung carcinomas (Shikada et al.). PDGF-AA also mediates proliferation of oligodendrocyte progenitor cells and oligodendrocyte lineage differentiation through the activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) (Hu et al.). PDGF-AA is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into oligodendrocyte precursor cells (Piao et al.).

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Macrophage colony-stimulating factor (M-CSF) is a homodimeric glycoprotein growth factor that regulates proliferation and differentiation of myeloid hematopoietic progenitor cells to mononuclear phagocytic cell lineages, including monocytes, macrophages, and osteoclasts. M-CSF is a crucial factor for the development of tissue-resident macrophages in most tissues (Ginhoux and Jung). It is required for the maturation and activation of monocytes and macrophages, and regulates inflammatory responses in conjunction with other stimuli such as IFN-γ, LPS, and IL-4 (Murray et al.). M-CSF is also required for bone resorption by osteoclasts, and is involved in the development and regulation of the placenta, mammary gland, and brain. M-CSF is produced by monocytes, fibroblasts, osteoclasts, stromal cells, endothelial cells, and tumor cells (Chockalingam and Ghosh). M-CSF exerts its biological effects by signaling through a receptor tyrosine kinase (CSF-1R or M-CSF-R) encoded by the c-fms proto-oncogene (Hamilton). CSF-1R shares similar structural features with other growth factor receptors, including the stem cell factor (SCF) receptor, platelet-derived growth factor receptor (PDGF-R), and Flt3/Flk-2 receptor tyrosine kinase. Stimulation of the CSF-1R upon binding to M-CSF activates MAPK, PI3K, and PLCγ signaling pathways (Chockalingam and Ghosh). Human and mouse M-CSF sequences are highly conserved both at nucleotide and amino acid levels (80% homology; DeLamarter et al.).

Supplier: STEMCELL Technologies

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 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. Recombinant human GM-CSF (rhGM-CSF) promotes the production of myeloid cells of the granulocytic (neutrophils, eosinophils and basophils) and monocytic lineages in vivo. It has been tested for mobilization of hematopoietic progenitor cells and for treating chemotherapy-induced neutropenia in patients. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.).

Supplier: STEMCELL Technologies

Interleukin 11 (IL-11) is a pleiotropic cytokine with effects on various tissues including the bone marrow, brain, and intestinal mucosa (Du and amp; Williams). It belongs to the IL-6 family of cytokines that share a common signal transducer, gp130. Culture of mouse bone marrow cells with IL-11 in combination with IL-3, IL-6, and stem cell factor induces significant expansion and proliferation of colony-forming cells in vitro (Peters et al.). In addition, in combination with IL-3, IL-11 significantly enhances the growth of megakaryocytic colonies in vitro, suggesting its role in augmenting mouse megakaryopoiesis (Yonemura et al.). IL-11 is expressed in a wide range of normal adult mouse tissues, including the central nervous system, thymus, lung, and bone. The mouse IL-11 cDNA was cloned using an expression library generated from the lipopolysaccharide-induced mouse fetal thymic cell line, T2 (Morris et al.). The binding of IL-11 to its receptor induces heterodimerization with the gp130 subunit and activation of JAK tyrosine kinases. IL-11 also plays a role in cancer progression by inducing the proliferation of epithelial cancer cells and the survival of metastatic cells at distant organs. Recently, IL-11 has gained interest for its role in the pathogenesis of diseases in dysregulated mucosal homeostasis associated with STAT3 upregulation, including gastrointestinal cancers (Putoczki et al.).

Supplier: STEMCELL Technologies

Interleukin 17A (IL-17A) is the founding member of the family of cytokines that includes Interleukin 17B through Interleukin 17F. It is a potent proinflammatory cytokine that plays a key role in defense against pathogens. IL-17A and IL-17F signal as homodimers or heterodimers through the same receptor, and activate NF-kB, MAPK, and C/EBP pathways (Gaffen). IL-17A receptor is expressed on a variety of cell types, including hematopoietic cell compartments. IL-17A is produced by T helper 17 cells, CD8+ T cells, γδ T cells, natural killer T cells, B cells, neutrophils, innate lymphoid cells and mesenchymal stromal cells (MSCs; Zenobia and amp; Hajishengallis; Mojsilovic et al.). IL-17A receptor is expressed at particularly high levels on stromal cells, including MSCs. IL-17A increases the frequency and the average size of colony-forming units-fibroblast derived from bone marrow, as well as the proliferation of bone marrow-derived MSCs. IL-17A suppresses osteogenic differentiation and bone formation of bone marrow-derived MSCs. The action of IL-17A on hematopoiesis is deeply reliant on the microenvironment and the induction of other regulators. In healthy mouse bone marrow, IL-17A stimulates myeloid and early stage erythroid progenitor cells but inhibits late stage erythroid progenitor cells (Mojsilovic et al.).

Supplier: STEMCELL Technologies

Stem cell factor (SCF) is an early-acting cytokine that plays a pivotal role in the regulation of embryonic and adult hematopoiesis. SCF promotes cell survival, proliferation, differentiation, adhesion, and functional activation of cells at multiple levels of the hematopoietic hierarchy. Together with other cytokines such as thrombopoietin and Flt3/Flk-2 Ligand, SCF is commonly used to promote expansion of primitive hematopoietic stem cells and multi-potent progenitor cells in culture (Huang et al.; Kent et al.). In synergy with various growth factors, including IL-2, IL-3, IL-6, IL-7, G-CSF, and erythropoietin, SCF increases proliferation and differentiation of myeloid and erythroid progenitor cells and a subset of lymphoid progenitor cells (Broudy). In the mouse, SCF is essential during fetal gonadal development (Mauduit). It is produced by stromal cells in the fetal liver, bone marrow, and thymus, in the central nervous system, in keratinocytes, and in the gut mucosa, and can function as a chemotactic and chemokinetic factor. SCF exists in two biologically active splice forms: a soluble and a transmembrane isoform. Upon binding to its receptor (c-kit tyrosine kinase receptor; CD117), it activates PI3K, JAK/STAT, and MAPK pathways. SCF and signaling from c-kit has also been reported to play an important role in pigmentation, fertility, vasculogenesis, motility of the gut via c-kit-positive interstitial cells of Cajal, and in the migration of neuronal stem and progenitor cells to sites of injury in the brain (Lennartsson and Ronnstrand).

Supplier: STEMCELL Technologies

Flt3/Flk-2 (Fms-like tyrosine kinase 3/fetal liver kinase-2) Ligand is a hematopoietic cytokine that plays an important role as a co-stimulatory factor in the proliferation, differentiation, and survival of hematopoietic stem and progenitor cells and the development of the immune system (Hannum et al.). Flt3/Flk-2 Ligand, together with stem cell factor and thrombopoietin, is commonly used to promote expansion of primitive CD34+ hematopoietic cells in culture. In combination with myeloid cytokines such as GM-CSF, G-CSF, or M-CSF, Flt3/Flk-2 Ligand enhances the growth and numbers of clonogenic myeloid progenitor cells. In synergy with the interleukins IL-3, IL-4, IL-7, IL-11, IL-12, IL-15, and GM-CSF and TNF-α, Flt3/Flk-2 Ligand regulates the development of various lymphoid progenitor cells, including dendritic cell, B cell, T cell, and NK cell progenitors. In contrast, Flt3/Flk-2 Ligand has no significant effect on erythropoiesis or megakaryopoiesis (Drexler and Quentmeier; Wodnar-Filipowicz). Flt3/Flk-2 Ligand exists as membrane-bound and soluble isoforms. Both isoforms are biologically active and signal through the class III tyrosine kinase receptor (Flt3/Flk-2, CD135; Rosnet et al.). Flt3/Flk-2 Ligand is produced by a variety of cell types, including uncommitted and committed hematopoietic cells and stromal fibroblasts, whereas expression of the Flt3/Flk-2 receptor is restricted to CD34+ hematopoietic stem and progenitor cells. Flt3/Flk-2 receptor is also expressed on leukemic cells and outside the hematopoietic system in the brain, placenta, and testis (Drexler and Quentmeier; Hannum et al.). This product is animal component-free.