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The EBV (BZLF1) peptide pool is a lyophilised mixture of 59 peptides from trans-activator protein BZLF1 of Epstein-Barr virus (EBV; strain B95-8). BZLF1 is a DNA-binding protein that acts as a switch from latent infection to lytic infection. The pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 245 on BZLF1.

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Interleukin 1 beta (IL-1β) is synthesised as an inactive precursor protein or pro-IL-1β. This precursor is cleaved intracellularly by Caspase 1 (IL-1β convertase) to form the active form of the protein that is later secreted (Allan et al.). IL-1β binds to IL-1 receptor and activates intracellular signaling via the MAPK or NF-kB pathway. IL-1β is released by monocytes, tissue macrophages, and dendritic cells in response to infection or injury and induces expression of acute-phase proteins. It also promotes the infiltration of inflammatory and immunocompetent cells from the circulation into the extravascular space and affected tissues, by stimulating the expression of adhesion molecules on endothelial cells. IL-1β also affects other immune cells; for example, it co-stimulates T cell functions together with antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner. This product is animal component-free.

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Amphiregulin is a member of the epidermal growth factor (EGF) family. It binds to several receptors including EGFR/ErbB1, HER2/ErbB2, HER3/ErbB3, and HER4/ErbB4, which activates Ras/Raf/MAPK and PI3K/AKT pathways. This results in cell proliferation, apoptosis resistance, and invasive behaviour (Normanno et al.). The expression of amphiregulin is induced by tissue injury and inflammation. Amphiregulin promotes mammary development, trophoblast growth, lung and kidney branching morphogenesis, and keratinocyte proliferation. It stimulates the growth of most cell types, including normal and transformed mammary epithelial cells, and malignant cells of the colon, prostate, cervix, and pancreas (Berasain and Avila).

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Interferon gamma-inducible protein (IP) 10 or CXCL10 is a member of the CXC chemokine family. It binds CXCR3 activating ERK1/2, p38/MAPK, JNK, and PI3-kinase/AKT signaling pathways, inducing intracellular calcium influx, DNA synthesis, cell proliferation, and chemotaxis. IP-10 regulates innate and adaptive immune responses by affecting the function of activated T cells, natural killer cells, inflammatory dendritic cells, macrophages, and B cells. IP-10 is produced by leukocytes, activated neutrophils, eosinophils, monocytes, epithelial cells, endothelial cells, fibroblasts, and keratinocytes in response to IFN-gamma. IP-10 has been implicated in a wide range of diseases, including infectious diseases and chronic inflammatory and autoimmune diseases, as well as in tumor formation (Liu et al.).

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

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Epidermal growth factor (EGF) is characterized by high-affinity binding to various EGF receptors (EGFRs) and the production of mitogenic responses (Carpenter and Cohen). EGF promotes EGFR dimerization, resulting in activation of downstream pathways including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signaling. EGF is secreted by the gut-associated salivary and Brunner’s glands, is found in a variety of body fluids, and stimulates cell proliferation and differentiation in rodent and neonatal human intestine (Wright et al.). Central nervous system stem cells also proliferate in response to the EGF stimulus (Reynolds and Weiss). This product is animal component-free.

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

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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Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes the proliferation and differentiation of hematopoietic progenitor cells and the generation of neutrophils, eosinophils, and macrophages. In synergy with other cytokines such as stem cell factor, IL-3, erythropoietin, and thrombopoietin, it also stimulates erythroid and megakaryocyte progenitor cells (Barreda et al.). GM-CSF is produced by multiple cell types, including stromal cells, Paneth cells, macrophages, dendritic cells (DCs), endothelial cells, smooth muscle cells, fibroblasts, chondrocytes, and Th1 and Th17 cells (Francisco-Cruz et al.). The receptor for GM-CSF (GM-CSFR) is composed of two subunits: the cytokine-specific α subunit (GMRα; CD116) and the common subunit βc (CD131) shared with IL-3 and IL-5 receptors (Broughton et al.). GM-CSFR is expressed on hematopoietic cells, including progenitor cells and immune cells, as well as non-hematopoietic cells. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.).

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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

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The platelet-derived growth factor (PDGF) family has five heparin-binding members that assemble into four homodimers (PDGF-AA, PDGF-BB, PDGF-CC, and PDGF-DD) and one heterodimer (PDGF-AB; Fretto et al.; Li and Eriksson). PDGF signals through the receptor tyrosine kinases PDGFRα and PDGFRβ. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src, and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin, such as fibroblasts, glial cells, and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-BB is secreted by osteoblasts to induce mesenchymal stem cell migration and angiogenesis. It has also been shown that PDGF-BB is secreted by preosteoclasts during bone modeling and remodeling to induce angiogenesis and thus proper osteogenesis (Xie et al.).

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils, and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation, and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) is a member of the EGF family (Nishi and Klagsbrun). HBEGF promotes blastocyst adhesion to the uterine wall (Iwamoto and Mekada). It also plays a role in smooth muscle cell hyperplasia and brain injury (Nishi and Klagsburn). HBEGF produced by CD4+ T cells promotes wound healing by stimulating migration and proliferation of keratinocytes, fibroblasts, and smooth muscle cells (Blotnick et al.). It binds to EGFR, ErbB4, ErbB2, and ErbB3, activating the PI3K/AKT signaling cascade (Iwamoto and Mekada). HBEGF is produced in a variety of cells, where it contributes to physiological and pathological processes. HBEGF is overexpressed in ovarian, breast, gastric, colorectal, pancreatic, and endometrial cancers, which likely contributes to pathogenesis (Miyata et al.). This product is animal component-free.

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Fibroblast growth factor 21 (FGF-21) is a member of the FGF family. Using β-Klotho as a cofactor, FGF-21 signals through FGF receptor 1c and 4 to activate PI3K and MAPK pathways (Mattila and Härkönen; Kharitonenkov et al.). FGF-21 expression is regulated by tissue-specific peroxisome proliferator-activated receptors (PPARs). Upon PPAR-α stimulation FGF-21 is produced in the liver, and activation of PPAR-γ leads to FGF-21 production in adipose tissue. FGF-21 promotes insulin-independent glucose uptake and lipid accumulation in primary human adipocytes and in mouse 3T3-L1 cells. In pancreatic islets and INS-1 cells it inhibits glucose-mediated glucagon release and stimulates insulin production. FGF-21 does not induce proliferation in immortalized cell lines, unlike other FGFs (Kharitonenkov and Shanafelt). FGF-21 regulates thermogenesis in white and brown adipose tissue, and metabolic processes in cells of pancreatic origin (Kharitonenkov et al.).

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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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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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The SARS-CoV-2 (NS8) Peptide pool is a lyophilised mixture of 28 peptides from non-structural protein 8 (NS8) of SARS-CoV-2. NS8 has been identified as one of the proteins exclusively conserved in a few species of the coronavirus family, and it contains Class II MHC epitopes. The pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 121 on NS8.

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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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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.).

Supplier: STEMCELL Technologies

Interferon-gamma (IFN-γ), also known as type II interferon, is produced by T and NK cells, and in smaller amounts by dendritic cells and macrophages. IFN-γ is controlled by cytokines such as IL-12 and IL-18 secreted in response to infection (Schroder et al.). IFN-γ binds to a receptor complex and initiates signal transduction via the JAK/STAT pathway; this culminates in the transcription and activation of many genes that control a diverse array of immunological functions (de Weerd and Nguyen; Krause et al.). IFN-γ stimulates the antimicrobial and anti-tumor activity of macrophages, NK cells, and neutrophils (Billiau and Matthys) by promoting the activation of microbial effector functions such as production of reactive oxygen species, NO intermediates, and complement (Schroder et al.). IFN-γ enhances MHC class I and II expression in dendritic cells and mononuclear phagocytes, as well as the production of IL-12 by dendritic cells. In B cells, IFN-γ stimulates survival and growth in both mouse and human cells, and redirects B cells from proliferation towards differentiation. IFN-γ favors the development of Th1 vs Th2 cells and stimulates monocyte differentiation and function (Schroder et al.). This product is animal component-free.

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 andamp; Williams). It belongs to the IL-6 family of cytokines that share a common signal transducer, gp130. IL-11 induces the proliferation of hematopoietic stem cells (Lemoli et al.) and megakaryocytic progenitor cells (Bruno et al.), the maturation of megakaryocytes (Burstein et al.), and the production of platelets (Neben et al.). IL-11 is produced by a variety of cell types including hematopoietic cells, mesenchymal cells, epithelial cells, and neuronal cells. It was first cloned from a cDNA library of the human bone marrow-derived stromal cell line KM-102 (Kawashima et al.). The binding of IL-11 to its receptor induces heterodimerization with the gp130 subunit and activation of JAK tyrosine kinases. IL-11 was the first pharmacologic agent approved for the treatment of chemotherapy-induced thrombocytopenia. 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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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 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 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). 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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Macrophage colony-stimulating factor (M-CSF) is a homodimeric cytokine that belongs to receptor tyrosine kinase subclass III of the receptor tyrosine kinase (RTK) family. M-CSF acts on a CSF-1 receptor tyrosine kinase, which initiates signaling cascades to support cell proliferation and differentiation (Hamilton). M-CSF is produced by endothelial cells, osteoblasts, and during pregnancy by the uterine epithelial cells (Ryan). M-CSF synergizes with other factors to support proliferation and differentiation of multipotent hematopoietic progenitor cells, and regulates proliferation and differentiation of the mononuclear phagocyte progenitor cells to monocytes and macrophages. It also supports survival, proliferation, and function of the differentiated macrophages and regulates differentiation of mononuclear phagocytes to osteoclasts (Pixley and Stanley). M-CSF plays an important role in the implantation of the embryo and early development (Makrigiannakis et al.).

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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.

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 andamp; Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilisation of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.

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

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Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes the proliferation and differentiation of hematopoietic progenitor cells and the generation of neutrophils, eosinophils, and macrophages. In synergy with other cytokines such as stem cell factor, IL-3, erythropoietin, and thrombopoietin, it also stimulates erythroid and megakaryocyte progenitor cells (Barreda et al.). GM-CSF was first purified from the culture of mouse lung tissue after lipopolysaccharide treatment. GM-CSF is produced by multiple cell types, including stromal cells, Paneth cells, macrophages, dendritic cells (DCs), endothelial cells, smooth muscle cells, fibroblasts, chondrocytes, and Th1 and Th17 cells (Francisco-Cruz et al.). The receptor for GM-CSF (GM-CSFR) is composed of two subunits: the cytokine-specific α subunit (GMRα; CD116) and the common subunit βc (CD131) shared with IL-3 and IL-5 receptors (Broughton et al.). GM-CSFR is expressed on hematopoietic cells, including progenitor cells and immune cells, as well as non-hematopoietic cells. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.).

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The SARS-CoV-2 (Nucleocapsid protein) Peptide pool is a lyophilised mixture of 102 peptides from the nucleocapsid protein of SARS-CoV-2. Nucleocapsid protein is one of four structural proteins that interacts with RNA to form the nucleocapsid. It also interacts with membrane protein (protein M) in the packaging of positive-strand viral genome RNA during virion assembly. The pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 419 on SARS-CoV-2 nucleocapsid protein.