You searched for: Proteins and Peptides

Supplier: STEMCELL Technologies

Stimulating T cells with CMV (HLA Class I Control) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. CMV Peptide pool is a lyophilised mixture of 14 peptides from the human cytomegalovirus (CMV) and consists of defined HLA class I-restricted T cell epitopes. Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development. For consistency and reproducibility across your applications, CMV Peptide pools from STEMCELL are formulated as lyophilised trifluoroacetate salts, with a purity ≥95%.

Supplier: STEMCELL Technologies

Myostatin is a member of transforming growth factor beta (TGF-β) superfamily that signals by binding to activin type II receptor, resulting in the recruitment of either ALK3 or ALK4 coreceptor, and activation of SMAD2/3 (Kondás et al.). It is released by myocytes and inhibits muscle growth and ability to regenerate (Lee and Lee). Myostatin appears to affect the lipid catabolic metabolism of adipocytes and inhibits preadipocyte differentiation, as demonstrated in the 3T3-L1 cell line (Li et al.).

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Tumor necrosis factor-beta (TNF-β), also known as lymphotoxin-alpha, is a member of the TNF family. It is a pro-inflammatory cytokine that activates NF-kB, MAPK, and PI3K/AKT pathways upon binding to TNF receptors 1 and 2. It is produced mainly by T cells, though other cells can express TNF-β at lower levels (Chu). TNF-β is involved in autoimmune disorders, lymph node development, and mediating the inflammatory demyelination process (Seleznik et al.; McCarthy et al.).

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Interleukin 5 (IL-5) is a member of the short-chain 4-α-helical bundle subset of hematopoietic cytokines. It binds to the specific α receptor, which in turn recruits the common β receptor that initiates signaling via JAK/STAT and MAPK pathways. IL-5 is produced by Th2 cells, eosinophils, activated mast cells, and ILC2 cells. IL-5 affects the differentiation, activation, and survival of eosinophils, thus playing an important role in allergic inflammation, asthma, and parasite immunity. Stimulation of eosinophils with IL-5 leads to their activation, upregulation of CD11b expression, and inhibition of apoptosis (Shearer).

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Insulin-like growth factor-binding protein 4 (IGFBP-4) inhibits the actions of IGF-I and IGF-II. The distribution of IGFBP-4 in tissues is dependent on its glycosylation state, however it preferentially targets connective tissue (Firth and Baxter; Qin et al.). IGFBP-4 is also produced in liver, adrenal glands, Leydig cells, developing embryos, spinal cord, and thymic cortex. IGFBP-4 inhibits WNT/β-catenin signaling, which downregulates prostate cancer proliferation (Zhu et al.). In vitro studies suggest that IGFBP-4 inhibits proliferation of neuroblastoma and glioma, while promoting bone loss in osteosarcoma and multiple myeloma (Durai et al.).

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Sonic hedgehog (Shh) is a member of the Hedgehog family of secreted signaling proteins that has a prominent role in patterning during early mammalian development (Ho and Scott). It is expressed during early embryogenesis in a variety of tissues (Finco et al.). During patterning of the central nervous system, Shh directly acts on cells to specify neural cell fates, regulates proliferation and survival of oligodendrocytes precursors and neural crest cells and stimulates proliferation, differentiation and axon growth (Ho and Scott; Martí). Shh also regulates T cell differentiation and activation (Crompton et al.). Recombinant human Shh (C24II; rhShh) is a fully biologically active molecule.

Supplier: STEMCELL Technologies

Conveniently and consistently add transforming growth factor beta 1 (TGF-ꞵ1) to your cultures with this cell culture-ready formulation. This human recombinant TGF-ꞵ1 is precisely reconstituted to 0,1 mg/ml in 100 mM acetic acid and requires no additional preparation, improving reproducibility. Endotoxin levels are verified, using the LAL method to ensure consistency for use across multiple applications. A member of the TGF-β superfamily, TGF-β1 regulates diverse cellular phenotypes. TGF-β1 binds to serine-threonine kinase type I and II receptors and activates signal transduction through SMAD2/3 proteins.

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Thrombopoietin (TPO) is a key regulator of megakaryocytopoiesis and thrombopoiesis in vitro and in vivo. TPO stimulates the proliferation and maturation of megakaryocytes and has an important role in regulating the level of circulating platelets in vivo. TPO also promotes the survival, self-renewal, and expansion of hematopoietic stem cells and primitive multilineage progenitor cells. It is commonly used with other cytokines such as stem cell factor (SCF) and Flt3/Flk-2 Ligand to promote expansion of primitive hematopoietic cells in culture (Hitchcock andamp; Kaushansky). The TPO receptor, c-Mpl, is expressed at all stages of megakaryopoiesis, from hematopoietic stem and progenitor cells to mature platelets.

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Fibroblast growth factor 5 (FGF-5) is a secreted, heparin-binding member of the FGF subfamily. FGFs possess broad mitogenic and cell survival activities and are expressed during embryonic development. FGF-5 is expressed in the mesenchyme, skeletal muscles, central nervous systems, and hair follicles. FGF-5 promotes cell differentiation and proliferation by binding FGF receptor 1 and FGF receptor 2 (FGFR1 and FGFR2, respectively). FGF-5 plays an important regulatory role in skeletal muscle development. FGF-5 has also been identified in neurons of the limbic system, especially those of the olfactory bulb and pyramidal cells of the hippocampus (Haub and Goldfarb).

Supplier: STEMCELL Technologies

A member of the SIBLING family of glycoproteins (Rangaswami et al.), Osteopontin (OPN) functions as T-helper 1 cytokine, and plays an important role in cell signaling, migration, and activation (Weber et al., 2002). Osteopontin has been shown to regulate inflammation both in vitro and in vivo (Agnholt et al.; Kiefer et al.), and has been implicated in the pathophysiology of numerous cancers, including prostate (Thalmann et al.), lung (Chambers et al.), ovarian (Kim et al.), and breast etiologies (Weber et al., 2015). In humans, OPN is initially secreted as a 317 amino acid protein which is subject to tissue-specific post-translational modifications by glycosylation, phosphorylation, and transglutamination (Kazanecki et al.; Sodek 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, Osteopontin from STEMCELL comes lyophilised with ≥92% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

Supplier: STEMCELL Technologies

Fetuin B is thought to have functions in female fertility, metabolism, and liver disease. A protease inhibitor belonging to the fetuin family of proteins, within the cystatin superfamily, fetuin b’s structure includes two cystatin domains (CY1 and CY2) connected by a linker, with a CPDCP-trunk and a C-terminal region (CTR) (Cuppari et al.). This plasma protein originates in the liver (Denecke et al.) and acts to inhibit the activity of ovastacin, a metalloprotease that causes the zona pellucida to harden, leading to female infertility (Karmilin et al.). Fetuin B has also been reported to increase apoptosis, and inhibit migration and invasion of prostate cancer cells, in in vitro and in vivo settings (Zhan et al.). Elevated serum fetuin B has been linked to non-alcoholic fatty liver disease (NAFLD) (Zhu et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apolipoprotein H 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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Tumor necrosis factor-α (TNF-α) is a pro-inflammatory cytokine that activates NF-kB, MAPK, and PI3K/AKT pathways. Activated T cells and macrophages are the primary producers of TNF-α in response to inflammation and infectious conditions. Many other cell types have been shown to produce TNF-α, among them B cells, NK cells, mast cells, neutrophils, dendritic cells, microglia, endothelial cells, smooth muscle cells, cardiomyocytes, and fibroblasts. TNF-α has cytotoxic effects on cancer cells in vitro by stimulating anti-tumor immuno- suppressive responses. TNF-α stimulates expression of E- and P-selectins, thus facilitating adhesion of neutrophils, monocytes, and memory T cells to activated platelets and endothelial cells (Zelová and Hosek). Other effects of TNF-α include vasodilatation and edema formation.

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Use sclerostin to alter bone remodeling homeostasis, where it inhibits bone formation in vivo and in vitro, likely through Wnt/β-catenin signaling cascades (Ellies et al.; Lin et al.). Sclerostin is a member of the cerberus/DAN family of glycoproteins whose members share a C-terminal cysteine-knot-like (CTCK) domain. Highly expressed in bone and cartilage, as well as in kidney, and liver tissues (Weivoda et al.), this osteoclast-derived BMP antagonist binds BMP6 and BMP7 with high affinity, and binds BMP2 and BMP4 with a lower affinity (Kusu et al.). Mutations in the SOST gene have been associated with sclerosteosis (Brunkow et al.), van Buchem disease (Staehling-Hampton et al.), and bone dysplasia disorders, characterized by increased bone density. This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

Modulate prostaglandin metabolism with 15-hydroxyprostaglandin dehydrogenase (15-PGDH). 15-PGDH catalyses the reversible oxidation of the 15-hydroxyl group in prostaglandins, resulting in inactivated metabolites (Ensor and Tai), it can act on a variety of prostaglandins as substrates in a NAD+ dependent manner (Cho et al.). As prostaglandins can have a range of effects on cellular processes, 15-PGDH is of considerable importance in drug development. In vitro and in vivo studies suggest 15-PGDH has tumor suppressive activity and is downregulated in certain cancers (Na et al.).15-PGDH belongs to the short-chain dehydrogenases/reductases (SDR) family; its primary structure indicates 20% homology with other SDRs, with some conserved amino acid residues (Krook et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apo M from STEMCELL comes lyophilised with ≥89% purity.

Supplier: STEMCELL Technologies

Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to the ST2 receptor and activates NF-kB and MAPK pathways. IL-33 is expressed by epithelial cells, smooth muscle cells, and fibroblasts in various tissues and organs, as well as resting basophils, mast cells, eosinophils, natural helper cells, group 2 innate lymphoid cells, dendritic cells, and activated macrophages (Schmitz et al.; Yasuda et al.). It contributes to allergic inflammation by stimulating production of the cytokines IL-4, IL-5, and IL-13 in Th2 cells, and stimulates host defense against microbial and viral infections (Liew; Yasuda et al.). In the central nervous system, IL-33 is produced by endothelial cells and astrocytes. It induces proliferation of microglia and mediates production of pro-inflammatory cytokines (Yasuoka et al.).

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Interleukin 13 (IL-13) is a type I cytokine, and signals through type I cytokine receptors to activate JAK/STAT and IRS-1/IRS-2 pathways. IL-13 is produced by T cells and innate lymphoid cells (Pulendran and Artis) and it inhibits production of pro-inflammatory cytokines, prostaglandins, and reactive oxygen and nitrogen species by monocytes and macrophages (Hershey). Unlike human B cells, IL-13 has no effect on mouse B cell development and function. IL-13 promotes eosinophil survival, activation, and recruitment, and also activates mast cells (Hershey). IL-13 regulates gastrointestinal parasite expulsion, airway hyperresponsiveness, allergic inflammation, tissue eosinophilia, goblet cell hyperplasia, intracellular parasitism, tissue remodeling, tumor cell growth, and fibrosis. IL-13 induces hypercontractility of smooth muscles by directly acting on the muscle cells as well as the enteric nerves (Wynn).

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Fibroblast growth factor 7 (FGF-7) is a member of the FGF family, and acts exclusively through a subset of FGF receptor isoforms expressed predominantly by epithelial cells (Finch and Rubin). FGF-7 seems to act specifically on epithelial cells and stimulates proliferation, migration, and differentiation of these cells, and also participates in epithelial protection and repair both in vitro and in vivo (Finch and Rubin; Werner). In contrast, FGF-7 is produced solely by cells of mesenchymal origin, and functions as a paracrine mediator of mesenchymal-epithelial communication (Rubin et al.). FGF-7 has also been shown to supplement several wound-healing properties of bioengineered skin (Erdag et al.) and to induce autophagy in human keratinocytes (Belleudi et al.). Additionally, FGF-7 has a role in pluripotent stem cell differentiation to endodermal pancreatic-like insulin-producing cells and thymic epithelial cells (Inami et al.; Niu et al.).

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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 (Jaye et al.; Galzie 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 CNS, 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 through protein kinase C and promotes cell survival by inhibiting p53 and proapoptotic signaling (Bouleau et al.).

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Interleukin 10 (IL-10) is the founding member of the IL-10 family of class II cytokines. All of the IL-10 cytokine family members have a four-helix bundle consisting of α-helical folds. Upon binding to its receptor, IL-10 activates signaling through JAK1 and STAT3. It is produced by dendritic cells, macrophages, and CD4+ T cells, as well as mast cells, NK cells, neutrophils, and B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the expression of pro-inflammatory cytokines and promote healing processes, and is important for the function of regulatory T cells. IL-10 also enhances B cell proliferation, immunoglobulin secretion, and class II MHC expression, while IL-10 produced by macrophages inhibits activation of neighboring macrophages, thus allowing a level of self-regulation (Ouyang 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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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.).

Supplier: Roth Carl

Gelatin

Supplier: Serva

Gelatin

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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.).

Supplier: Roth Carl

Casein alcalisoluble

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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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Phosphoramidon (disodium salt)

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Interleukin 34 (IL-34) is well known for its ability to induce the formation of colony-forming unit macrophages in human bone marrow cell cultures (Foucher et al.; Wei et al.). This dimeric glycoprotein is a member of the short-chain helical hematopoietic cytokine family (Baghdadi et al.; Foucher et al.), and exists in two isoforms that differ by a single glutamine (Chen et al.; Foucher et al; Wei et al.). IL-34 interacts with M-CSF to trigger tyrosine phosphorylation of the receptor and ERK1/2 pathways. (Wang et al.; Wei et al.). It is expressed in many tissues (heart, brain, lung, liver, kidney, thymus, testes, ovary, small intestine, prostate, and colon), with the highest expression in the spleen. In combination with RANKL, IL-34 induces osteoclast differentiation (Chen et al.; Foucher et al.). IL-34 expression is decreased in Alzheimer’s disease and atopic dermatitis, while high levels of IL-34 are found in many types of cancer correlated with poor prognosis, chronic heart failure or coronary artery disease, inflammatory bowel disease, influenza A infection, during acute liver transplant rejection or in non-alcoholic fatty liver disease, and with rheumatoid arthritis (Baghdadi et al.). It is therefore a possible pharmacological target for treating bone or inflammatory diseases (Chen et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain, and the protein was purified as a homodimer consisting of 39 kDa monomers (Lin et al.).