31851 Results for: "Sodium+ionophore+II"

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

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

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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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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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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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Use angiopoietin-like protein 2 (ANGPTL2) to regulate tissue remodeling through integrin α5β signaling and activation of p38 mitogen-activated protein kinases (MAPK) (Odagiri et al.; Tabata et al.). Highly expressed in the heart, small intestine, and stomach, ANGPTL2 is a glycosylated secretory protein that contains a coiled domain and a fibrinogen-like domain (Kim et al.). Studies have shown that the coiled-coil domain of ANGPTL2 functions as a growth factor, enhancing the survival of hematopoietic stem cells (HSCs) ex vivo (Broxmeyer et al.). ANGPTL2 is also known to play a role in obesity and metabolic diseases, promoting local inflammation in adipose tissue and systemic insulin resistance in mice models (Tabata et al.). By activating an inflammatory cascade in endothelial cells and increasing macrophage infiltration, ANGPTL2 accelerates vascular inflammation which may lead to endothelial dysfunction and atherosclerosis progression (Horio et al.). This protein product contains a His-residue tag at the amino end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥92% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Interleukin 17A (IL-17A) is the founding member of the family of cytokines that includes IL-17B through IL-17F. It is a potent pro-inflammatory 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-κB, MAPK, and C/EBP pathways (Gaffen). IL-17A is produced by Th17 cells, CD8+ T cells, γ/δ T cells, natural killer (NK) T cells, B cells, innate lymphoid cells, and mesenchymal stromal cells (MSCs) (Cua and Tato; Gaffen; Mojsilović et al.). IL-17A mediates protection against extracellular pathogens, and together with IL-22 stimulates production of antimicrobial peptides. It induces granulopoiesis factors and neutrophil-specific chemokines. Together with tumor necrosis factor alpha (TNF-α), IL-17A induces a sustained neutrophil recruitment during inflammation (Cua and Tato). IL-17A receptor is expressed at particularly high levels on stromal cells, including MSCs. IL-17A increases the frequency and the average size of fibroblast colony-forming units (CFU-F), as well as the proliferation of marrow-derived MSCs. It enhances osteogenic differentiation, and inhibits adipocyte differentiation and chondrogenesis (Mojsilović et al.).

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Dickkopf-related protein 1 (DKK-1) is a member of the Dickkopf family and is a secreted protein that inhibits the canonical WNT pathway by competitive binding to low-density lipoprotein receptors (LRP)-5 and 6 with high affinity, thereby decreasing β-catenin protein stability (Niehrs). DKK-1 regulates embryonic development and contains two conserved cysteine-rich domains separated by a linker region and an N-terminal signal peptide (Krupnik et al.; Lieven et al.). A family of human DKK-related genes composed of DKK-1, DKK-2, DKK-3, and DKK-4 have been characterized together with a unique DKK-3 related protein termed Soggy (Krupnik et al.). DKK-1 has been shown to support the generation of myeloid-derived suppressor cells (MDSCs) and thus is a negative regulator of antitumor immune responses (D’Amico et al.). DKK-1 from thrombocytes is an important regulator of leukocyte infiltration and induces Th2 cell polarization and potentiates Th2 cell cytokine expression (Chae et al.). DKK-1 has also been shown to drive cardiac and retinal differentiation from induced pluripotent stem (iPS) cells (Lian et al.). Protein contains a His-residue tag at the carboxyl end of the polypeptide chain.

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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 alpha 1 (IFNA1) belongs to the type 1 interferon family of cytokines, which bind interferon alpha receptors (IFNAR; composed of IFNAR1 and IFNAR2 subunits) that are involved in interferon-induced JAK-STAT signaling (Shemesh et al.). Interferons have inhibitory effects on viral replication and pathogenesis, and studies have found that IFN alpha can prevent the spread of herpes simplex virus (HSV) (Mikloska and Cunningham), and human immunodeficiency virus (HIV) (George and Mattapallil). Pegylated forms of IFN alpha are currently approved for the treatment of chronic hepatitis B (Woo et al.). IFN alpha also displays anti-tumor effects by regulating cell growth and proliferation, and it is used in the treatment of different cancers (Tagliaferri et al.). Interferons display alpha-helical structures with four helices forming an antiparallel alpha-helix bundle (Walter). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, interferon alpha 1 from STEMCELL comes lyophilised with ≥90% purity, specific activity EC50 ≤40 to 200 pg/ml, and LAL analysis verification ensuring endotoxin levels are ≤1,0 EU/μg protein.

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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.

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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 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.).

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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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Complement factor D is a component of the alternative pathway of the complement system and part of the innate immune system, playing a vital role in the initiation and amplification of complement activation, in order to defend against infection (Barratt and Weitz). A serine protease belonging to the S1 peptidase family, complement factor D is secreted by adipocytes into circulating blood, and is also expressed by macrophages and monocytes (White et al.). In the initiation phase of the complement pathway, complement factor D cleaves complement factor B (bound to component C3) to produce a complex known as C3 convertase. During the amplification phase, complement factor D cleaves complement factor B (bound to component C3b) to produce the C3bBb convertase, and is involved in the propagation of complement activation. In addition to its immunological role, complement factor D is involved in other physiological processes, such as the efficient clearing of damaged cell debris by phagocytes following acute liver injury (Cresci et al.). Complement factor D deficiency is associated with an increased susceptibility to pathogens like Neisseria meningitidis (Biesma et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, complement factor D from STEMCELL comes lyophilised with ≥94% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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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.).

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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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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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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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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.

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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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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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.

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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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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.

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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.).

Supplier: STEMCELL Technologies

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.).

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 (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.

Supplier: VELP SCIENTIFIC

The UDK Series distillers are designed to meet the most challenging demands and requirements for diverse applications, according to international standards: Kjeldahl nitrogen TKN, proteins, ammoniacal nitrogen, nitric nitrogen (Devarda), phenols, TVBN and volatile acids, cyanides, and alcohol content. Five different UDK models are available with different automation levels to match any laboratory requirement of automation and throughput. A complete range of distillers featuring exclusive technologies to meet any laboratory requirement for the determination of analytes in different fields of application.

Supplier: STEMCELL Technologies

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.).