You searched for: Proteins and Peptides

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Use visfatin to catalyse the production of nicotinamide mononucleotide from nicotinamide (Revollo et al.). Nicotinamide mononucleotide is a precursor to nicotinamide adenine dinucleotide (NAD) that is vital to energy metabolism, cell death, and other cellular processes (Ying). Visfatin also acts as an immunomodulator by activating leukocytes and inducing the production of pro-inflammatory and anti-inflammatory cytokines (Moschen et al.), and there is evidence that visfatin can regulate insulin receptor signaling and insulin secretion (Brown et al.). Belonging to the nicotinate phosphoribosyltransferase (NAPRTase) family, Visfatin is an adipokine that is produced in adipocytes, leukocytes, and hepatocytes (Chiu et al., Garten et al., Kralisch et al.). It is active as a homodimer with each identical monomer consisting of two structural domains made up of 19 β-strands and 13 α-helices (Kim et al.). For consistency and reproducibility across your applications, visfatin from STEMCELL comes lyophilised with ≥90% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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Nerve growth factor (NGF)-beta is a prototypical member of the neurotrophin family and has a role in the survival and growth of neural cells, regulating cell growth, promoting differentiation into neurons, and neuron migration. The beta subtype of NGF is biologically active in comparison to the alpha-2 and gamma-2 subtypes. NGF-beta in its secreted form can bind to tyrosine kinase A (trkA) receptor with high affinity and to p75 (NTR) with low affinity (Levi and Alemà; Sofroniew et al.). NGF has been shown to possess pro-inflammatory and pro-fibrogenic properties (Micera et al.). It has also been shown that overexpression of NGF-beta promotes differentiation of bone marrow mesenchymal stem cells into neurons through regulation of AKT and MAPK pathways (Yuan et al.). This product is animal component-free.

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Vascular endothelial growth factor C (VEGF-C) is a member of the VEGF/platelet-derived growth factor (PDGF) family of proteins. VEGF-C is a potent angiogenic factor and promotes lymphangiogenesis, endothelial cell growth and survival, and can affect blood vessel permeability. VEGF-C is expressed in a range of tissues, but is not expressed in peripheral blood lymphocytes. VEGF-C forms a non-covalent, cell surface-associated, disulfide-linked homodimer that can bind and activate VEGF receptors 2 (VEGFR-2 [Flk1]) and 3 (VEGFR-3 [Flt4]). Interaction with VEGFR-2 results in physiological and intratumoral neoangiogenesis and vessel sprouting (Cao et al.; Tammela et al.), whereas interaction with VEGFR-3 is critical for lymphangiogenesis (Karkkainen et al.; Laakkonen et al.; Mäkinen et al.). Overexpression of VEGF-C in tumor cells has been shown to result in enhanced lymph flow and increased metastasis to regional lymph nodes (Hoshida et al.; Mandriota et al.; Padera et al.; Skobe et al.).

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Interleukin 15 (IL-15) is a four-alpha helix bundle cytokine with many similar properties to IL-2. 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 naïve 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.). This product is animal component-free.

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

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Butyrophilin 1A1 (BTN1A1) is a glycoprotein belonging to the butyrophilin (BTN) family which collectively modulates immune responses, through excitatory and inhibitory signals targeting immune cells. Butyrophilins are composed of two extracellular immunoglobulin domains and a transmembrane region, with a conserved B30.2 domain (PRYSPRY) that is present in most members (Malinowska et al.). BTN1A1, along with BTN2A2, has been shown to inhibit the proliferation of CD4+ and CD8+ T cells, modify T cell metabolism, and affect the expression of IL-2 and IFN-γ (Smith et al.). Due to these modulatory effects on T cells, BTN1A1 may have a role in inhibiting the development of autoimmune diseases (Stefferl et al.). BTN1A1 is also expressed in mammary glands and is required for the secretion of milk lipids during lactation (Ogg et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, Serpin A12 from STEMCELL comes lyophilised with ≥92% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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

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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 embryonic stem cells (Xu et al.; Kang et al.), stimulates human embryonic stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga 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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Vascular endothelial growth factor (VEGF-165) is a heparin-binding homodimeric glycoprotein involved in embryonic vasculogenesis and angiogenesis. VEGF binds to VEGFR-1 (R1) and VEGFR-2 (R2), and activates Raf/MEK/ERK and PI3K/AKT pathways (Ferrara et al.). It 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 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.). VEGF-165 contains two polypeptide chains of 165 amino acids each. This product is animal component-free.

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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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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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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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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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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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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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Use hepassocin to bind to lymphocyte-activation gene 3 (LAG-3) in an MHC class II independent manner, and inhibit antigen-specific T-cell activation (Wang et al.). Hepassocin is known to play a restorative role in the liver, reducing apoptosis and accelerating hepatocyte proliferation in vivo (Li et al.). In addition to these hepatoprotective effects, studies have shown that hepassocin expression is upregulated in gastric cancer tissues (Zhang et al.) and in breast cancer cells (Du et al.), suggesting it has potential to predict cancer disease progression. Hepassocin is a member of the fibrinogen superfamily, whose members share a fibrinogen domain at their C-terminus. It is predominantly expressed in the liver, and weakly in the pancreas (Hara et al.), and is secreted as a homodimer that consists of 312 amino acids. Hepassocin is an acute-phase reactant whose expression in HepG2 cells has been shown to be regulated by IL-6 (Liu and Ukomadu). This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, hepassocin from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

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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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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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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, bone formation and resorption (Sims and Quinn; Tanaka and Miyajima).

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

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

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CD40 ligand is a type II transmembrane glycoprotein that belongs to the tumor necrosis factor (TNF) superfamily (Quezada et al.). CD40 ligand forms a bioactive homotrimer that exists as both soluble and membrane-bound forms (Khandekar et al.). CD40 ligand is expressed on T cells, monocytes, basophils, eosinophils, platelets, dendritic cells, and endothelial cells. Its receptor, CD40, is expressed on B cells, dendritic cells, macrophages, monocytes, platelets, endothelial cells, and epithelial cells (van Kooten and Banchereau). Binding of CD40 ligand to CD40 stimulates B cell proliferation, immunoglobulin class switching, antibody secretion, and T cell-dependent humoral responses. Dysregulation of CD40 ligand contributes to immune deficiency in HIV and AIDS (Rickert et al.). CD40 ligand has also been linked to the pathology of atherosclerosis, atherothrombosis, and restenosis (Hassan et al.).

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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.). This product is animal component-free.

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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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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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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.