You searched for: Proteins and Peptides

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The B18R protein, which is encoded by the B18R open reading frame in the Western Reserve (WR) strain of vaccinia virus, is a type I interferon (IFN)-binding protein that is known to inhibit IFN antiviral response (Colamonici et al.). B18R protein has been shown to exhibit neutralizing activity to type I interferon family members (Meyers et al.) and to protect cells from the antiviral effects of interferon (Vancová et al.). It was recently shown that HIV-1–dependent induction of type I IFN activity and BAFF protein levels was abrogated by the soluble B18R protein, with no effect observed on the cell viability (Gomez et al.). B18R protein has been reported to aid in cellular reprogramming using RNA-mediated gene delivery (Warren et al.; Yoshioka N et al.).

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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.

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Noggin binds to and antagonizes bone morphogenetic protein (BMP) ligands of the transforming growth factor beta (TGF-β) family. Noggin supports maintenance of undifferentiated human embryonic stem cells cultured in mouse embryonic fibroblast (MEF)-conditioned medium (Chaturvedi et al.), and promotes dopaminergic differentiation of embryonic stem cells and subsequent survival of dopamine neurons (Chiba et al.). Noggin is essential for development of ectodermal structures including neural tube, tooth, hair follicle, and eye, as well as patterning of mesodermal somites and skeletal structures. It also influences chondrogenesis, osteogenesis, and joint formation (Krause et al.).

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Insulin-like growth factor 2 (IGF-II) is a polypeptide that belongs to the family of insulin-like growth factors that are similar in molecular structure to proinsulin. IGF-II binding to IGF-I receptor activates a signaling cascade via the MAPK and PI3K pathways. IGF-II affects growth, differentiation, and survival of cells in a variety of tissues during embryonic development. It stimulates proliferation and migration of primary lymphatic endothelial cells, and induces lymphangiogenesis (Guvakova).

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A member of the pentraxin family of proteins, C-reactive protein (CRP) plays important roles in host defenses, including regulating complement activation in vivo (Sjoberg et al.), decreasing nitric oxide production, and inhibiting angiogenesis in vitro (Verma et al., 2002). At specific concentrations, CRP directly inhibits endothelial progenitor cell (EPC) differentiation, survival, and function, and is thus implicated in the development of cardiovascular diseases (Verma et al., 2004). CRP is primarily synthesized by liver hepatocytes, but also by other immune cells, such as macrophages and lymphocytes (Sproston and Ashworth). The expression of this acute-phase protein is induced by IL-6 and IL-1 secretion of macrophages and T-cells during inflammation. For consistency and reproducibility across your applications, C-reactive protein from STEMCELL comes lyophilised with ≥87% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

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Use omentin for the maintenance of insulin sensitivity and metabolism, decreasing levels of this adipokine have been associated with obesity, insulin resistance, and diabetes (Tan et al.). Studies have suggested that omentin may have protective effects against atherosclerosis, arterial calcification, and myocardial injury through AMP-activated protein kinase (AMPK) and Akt-dependent mechanisms (Xu et al., Kataoka et al.). Through regulation of Sirt1-dependent p53 deacetylation, omentin can inhibit proliferation and induce apoptosis in hepatocellular carcinoma cells (Zhang and Zhou). Omentin is mainly produced by visceral adipose tissue, but is also expressed in the small intestine, colon, mesothelial cells, vascular cells, and plasma (Watanabe et al). Protein sequence analysis has shown that omentin comprises 313 amino acids, with a secretory signal sequence and fibrinogen-related domain (Yang et al.). For consistency and reproducibility across your applications, Omentin from STEMCELL comes lyophilised with ≥90% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤5,0 EU/μg protein.

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

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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. 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 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to a heterotrimeric receptor 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.). Targeted deletions of the IL-2 gene in mice resulted in development of autoimmune hemolytic anemia, followed by ulcerative colitis. Similar effects were observed in mice that were deficient in IL-2 receptor α (Gaffen and Liu).

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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).

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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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Epidermal growth factor (EGF) is the founding member of the EGF family of proteins and 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.). EGF can stimulate the proliferation of mouse embryonic stem cells or induce the terminal differentiation/growth inhibition of A431 cells (Heo et al.).

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Noggin binds to and antagonizes bone morphogenetic protein (BMP) ligands of the transforming growth factor beta (TGF-β) family. Noggin supports maintenance of undifferentiated human embryonic stem cells in vitro, and can be used to prevent spontaneous differentiation in the short term (Chaturvedi et al.). Noggin is essential for development of structures derived from ectoderm embryonic somite, skeletal patterning, and neurogenesis in vivo. It also influences chondrogenesis, osteogenesis, and joint formation (Krause et al.), and promotes dopaminergic differentiation of embryonic stem cells and subsequent survival of dopamine neurons (Chiba et al.).

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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. Mice deficient in IL-1β do not show phenotypical differences from wild-type mice; however, they have a reduced response to inflammation, suggesting that IL-1β plays a key role in inflammatory diseases (Dinarello).

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Interleukin 22 (IL-22) is a class 2 α-helical cytokine that signals through the class 2 cytokine receptor and activates the JAK/STAT pathway. IL-22 is secreted by Th1, Th2, Tc22, and γδ T cells, dendritic, mast and NK cells. It stimulates expression of antimicrobial peptides from epithelial cells, thus hindering bacterial infections. Depending on the interactions with other cytokines, IL-22 can either promote inflammation or prevent tissue destruction by regulating host defense and tissue homeostasis at barrier surfaces (Sonnenberg et al.).

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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).

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SARS-CoV-2 Recombinant Nucleocapsid Protein, aa1-419 is expressed in E. coli and is one of four structural proteins encoded by the SARS-CoV-2 genome. The Nucleocapsid Protein is transcribed from the viral “N” gene and is the protein that interacts with RNA to form the nucleocapsid. The protein is a homo-oligomer, and both the monomer and the oligomer can interact with RNA. This protein also interacts with the membrane protein (protein M) after infection of the host cell during packaging of the positive-strand viral genome RNA into the ribonucleocapsid during virion assembly. At the amino terminus, SARS-CoV-2 Recombinant Nucleocapsid Protein contains a thrombin site, a T7 tag, and a polyhistidine tag.

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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.

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Vascular endothelial growth factor (VEGF-165) is a heparin-binding homodimeric glycoprotein involved in embryonic vasculogenesis and angiogenesis. VEGF binds to VEGFR-1 (R1) and VEGFR-2 (R2), and activates Raf/MEK/ERK and PI3K/AKT pathways (Ferrara et al.). It plays an important role in neurogenesis both in vitro and in vivo (Storkebaum et al.). It has neurotrophic effects on neurons of the central nervous system and promotes growth and survival of dopaminergic neurons and astrocytes. VEGF also promotes growth and survival of vascular endothelial cells, monocyte chemotaxis, and colony formation by granulocyte-macrophage progenitor cells (Ferrara et al.).

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Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including mast cells, basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Fung et al.; Metcalf 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 mast cells, basophils and eosinophils. The mouse IL-3 receptor consists of a unique alpha-subunit (CD123) and two beta subunits, one specific for IL-3 (βIL-3), the other shared with the receptors for IL-5 and GM-CSF (beta common chain, βc or CD131). IL-3 binding to heterodimeric receptors containing the alpha subunit and one of either beta subunits activates JAK/STAT, MAPK, and PI3K signaling pathways (Scott and Begley).

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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 T regulatory 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.). This product is animal component-free.

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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 the differentiation of pluripotent stem cell to endodermal pancreatic-like insulin-producing cells and thymic epithelial cells (Inami et al.; Niu et al.). This product is animal component-free.

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Interleukin 1 receptor antagonist (IL-1RA) is a member of the IL-1 family that binds to IL-1 receptors but does not induce any intracellular signaling (Arend et al.). IL-1RA is a natural regulator of IL-1’s biological activity. It binds to the IL-1 receptors with similar affinity as IL-1, thereby inhibiting the proinflammatory activities of IL-1ɑ and IL-1ꞵ (Kinne et al.). In particular, mesenchymal stem cells have been shown to enhance tissue repair in an IL-1RA-dependent manner through the suppression of IL-1ꞵ production in dermal macrophages and enhanced expansion of immunosuppressive regulatory T cells in the skin (Harrell et al.). IL-1RA has also been shown to help in the treatment of rheumatoid arthritis (Cutolo), sepsis, asthma (Mao et al.), and inflammatory bowel diseases (Dosh et al.). This product is animal component-free.

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Vascular endothelial growth factor (VEGF-121) is a naturally-occurring VEGF-A splice variant involved in embryonic vasculogenesis and angiogenesis. VEGF binds to VEGFR-1 and VEGFR-2, and activates Raf/MEK/ERK and PI3K/AKT pathways. VEGF-121 is released as a freely diffusible protein by a variety of normal and transformed cells. It plays an important role in neurogenesis both in vitro and in vivo (Storkebaum et al.). It has neurotrophic effects on neurons of the central nervous system and promotes growth and survival of dopaminergic neurons and astrocytes. VEGF also promotes growth and survival of vascular endothelial cells, monocyte chemotaxis, and colony formation by granulocyte-macrophage progenitor cells (Ferrara et al.).

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Interleukin 7 (IL-7) is a member of the type I cytokine family that is critical for T and B cell development and survival. It is produced by non-hematopoietic cells in the thymus, lymphoid organs, and by bone marrow stromal cells (Lundström et al.). IL-7 binds to a receptor composed of common gamma chain and IL-7Ra (CD127) and signals through the JAK/STAT and PI3K pathways. IL-7 regulates the survival of naïve and memory CD4+ and CD8+ T cells, γδ T cells, NK T cells, innate lymphoid cells, and T regulatory cells (Carrette and Surh), and provides signals to promote survival, proliferation, and differentiation during B cell development (Clark et al.; Corfe and Paige).

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Interleukin 1 beta (IL-1β) is synthesized 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-κB 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 an antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner.

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A member of the apolipoprotein family, Apolipoprotein A-I (apo A-I) is a major glycoprotein component of high density lipoprotein (HDL) particles (Frank and Marcel) which facilitate the reverse transport of cholesterol from peripheral tissues to the liver. Apo A-I binds to the scavenger receptor SR-A1, allowing HDL particles to interact with cells in peripheral tissues (Neyen et al.), and is involved in the esterification of cholesterol, acting as a cofactor for lecithin cholesterol acyltransferase (LCAT; Frohlich). Apo A-I has been shown to bind to the scavenger receptor SR-B1 (Williams et al.) and the beta chain of ATP synthase (Martinez et al.) on hepatocytes, highlighting its importance in HDL endocytosis. Mutations in the APOA1 encoding gene may result in dysregulated HDL levels, leading to an increased risk of amyloidosis and ischemic heart disease (Haase et al.; Obici et al.). This protein product contains a His-residue tag at the amino end of the polypeptide chain. 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.

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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.