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A cytokine belonging to the type 1 interferon family, Interferon beta (IFN beta) binds IFN alpha/beta receptors (IFNAR) that activate tyrosine kinases and initiate the interferon-induced Jak-STAT signaling pathway, which modulates many key immune processes (Smieja et al.). In an experimental model involving cardiac fibroblasts isolated from rats, IFN beta was found to induce both pro- and anti-inflammatory cytokines production by activating different STAT proteins (Bolivar et al.). The anti-inflammatory effects of IFN beta have been studied in the context of autoimmune disorders, and there are currently multiple approved IFN beta drugs for treatment of relapsing forms of multiple sclerosis (Filipi and Jack). IFN beta is produced by immune cells, including macrophages, and non-immune cells, such as fibroblasts and epithelial cells (Ivashkiv and Donalin). The crystal structure of IFN beta shares characteristics with other type I interferons. It comprises five alpha-helices with four of them forming a helix bundle, and one long and three shorter loops connecting the helices (Karpusas et al.). For consistency and reproducibility across your applications, interferon alpha 1 from STEMCELL comes lyophilised with ≥87% purity, specific activity EC50 ≤18 pg/mL, and LAL analysis verification ensuring endotoxin levels are ≤1,0 EU/μg protein.

Supplier: STEMCELL Technologies

Interleukin 15 (IL-15) is a four-alpha helix bundle cytokine with many similar properties to IL-2. The IL-15 receptor is a heterotrimeric receptor composed of IL-15Ra (the high-affinity receptor for IL-15), as well as IL-2/15Rb (CD122) and common gamma chain (CD132). IL-15 binds to IL-15Rα receptor and can then be presented in trans to IL-2/15Rb and common gamma chain on other cells. Trans-presentation is thought to be the major mechanism by which IL-15-mediated responses occur in mice, although may not be necessary in humans (Castillo et al.). The cytoplasmic domains of IL-2/15Rb and common gamma chain mediate signaling to activate JAK/STAT and PI3K pathways. IL-15 supports the survival and proliferation of naïve CD4+ and CD8+ T cells, and promotes homeostasis of memory T cells. IL-15 also promotes the survival and differentiation of NK cells and regulates their cytolytic activity (Ma et al.). This product is animal component-free.

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Fibroblast growth factor 10 (FGF-10) is a member of the fibroblast growth factor (FGF) family predominantly expressed by mesenchymal fibroblasts during embryonic development (Emoto et al.; Igarashi et al.). It binds with high affinity to fibroblast growth factor receptor 2-IIIb (FGFR2-IIIb), and also has a weaker affinity for FGFR1-IIIb (Beer et al.). FGF-10 and FGF-7 have similar receptor binding properties and target cell specificities but are differentially regulated by components of the extracellular matrix (Emoto et al.; Igarashi et al.). FGF-10 has been shown to mediate epithelial-mesenchymal interactions, which are essential to lung development (Sekine et al; Ware and Matthay). FGF-10 also has a role in mobilisation and proliferation of lung-resident mesenchymal stem cells (MSCs) and protection and repair against acute lung injury (Tong et al.; Ware and Matthay), as well as endodermal differentiation of human pluripotent stem cells to insulin-producing pancreatic-like cells (Takeuchi 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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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

Stimulating T cells with EBV (GP350/340) Peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. EBV (GP350/340) Peptide pool is a lyophilised mixture of 224 peptides from envelope glycoprotein GP350 (GP350/340) of Epstein-Barr virus (EBV; strain B95-8), and consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 907 on GP350/340. GP350 meditates EBV attachment to B lymphocytes via binding to the cell surface receptor CR2 (also known as C3d receptor or CD21) (Nemerow et al.; Tanner et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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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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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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Colistin sulphate

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Soy bean trypsin inhibitor

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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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FRET-based peptide substrate for detection of protease activity of coronaviruses - 1000 tests.

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Bovine serum albumin (BSA), Fraction V

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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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Fluorescent dye conjugates for detection of F-actin in cell culture experiments - 300 tests.

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Fluorescent dye conjugates for staining cell membranes of gram-positive bacteria, mammalian cells, and yeast bud scars - 1000 µg.

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Epidermal growth factor receptor (EGFR) is a type I transmembrane protein and receptor tyrosine kinase. EGFR has been shown to bind to some members of the EGF family ligands including EGF, amphiregulin, TGF-α, betacellulin, epiregulin, heparin-binding EGF, and neuregulin-2α. EGFR ligand binding induces homodimerization, as well as heterodimerization of EGFR with ErbB2 or with ligand-activated ErbB3 or ErbB4 (Schlessinger). Dimerization results in kinase activation, phosphorylation, and cell signaling, mediated primarily through MEK/ERF and AKT pathways (Navlonic et al.). EGFR signaling has been shown to regulate cell proliferation, differentiation, motility, and apoptosis. Elevated levels of EGFR have been correlated with carcinogenesis (Maihle et al.). Protein contains a His-residue tag at the carboxyl end of the polypeptide chain.

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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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Transforming growth factor (TGF) beta 3 is a member of the TGF-β superfamily and regulates diverse cellular phenotypes. TGF-beta 3 binds to serine-threonine kinase type I and II receptors and activates signal transduction through SMAD2/3 proteins, thus regulating a variety of functions, including cell proliferation, differentiation, wound healing, apoptosis, and metabolism (Massagué; McDowell et al.). TGF-beta 3 enhances glycosaminoglycan production by mesenchymal stromal cells, stimulates scar-free healing, and improves glucose tolerance and phenotypic changes in adipocyte morphology (Hall et al.; Holton et al.). TGF-beta 3 induces proliferation of posterofrontal suture-derived mesenchymal stromal cells, and stimulates expression of fibroblast growth factors 2 and 18 (James et al.).

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Hepatocyte growth factor/scatter factor (HGF/SF) is a pleiotropic growth factor that promotes proliferation, motility, survival, and differentiation. HGF binds and promotes the dimerization and activation of the receptor tyrosine kinase c-MET, and stimulates PI3K/AKT, FAK, JNK, and ERK1/2 signaling (Organ and Tsao). HGF stimulates migration of cells during embryogenesis, induces cell motility and scattering of epithelial cells, and regulates epithelial-mesenchymal transition. It is a chemoattractant for motor neurons, and regulates the development of sensory, sympathetic, parasympathetic, and cortical neurons as well as the proliferation of oligodendrocytes and glial development. Additionally, HGF is cytoprotective and regulates liver growth and regeneration (Nakamura et al.).

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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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Interferon-alpha (IFN-α) is a type I interferon, produced by virus infected cells, and is released as a soluble factor to initiate antiviral responses (Isaacs and Lindenmann). IFN-α2 is the most potent IFN-α used in fundamental research and in most clinical applications. The best known IFN-α2 subvariants, 2A and 2B, differ by only one or two amino acids at positions 23 and/or 34 of the mature protein (von Gabain et al.). Type I IFNs exert potent antitumor activity by increasing the cytotoxic activity of NK and T cells, as well as inhibiting the proliferation of cancer cells (Paul et al.). Additionally, it has been shown that proinflammatory IFN-α modulates the function of B cells in patients with systemic lupus erythematosus (Chang et al.) and pegylated form of IFN-α 2A and 2B has implications in the treatment of Hepatitis C (Foster et al.).

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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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Gelatin

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Chymostatin

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Antipain

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B cell activating factor (BAFF) is part of the tumor necrosis factor (TNF) superfamily and is expressed by monocytes, macrophages, dendritic cells, and neutrophils (Mackay and amp; Browning; Scapini et al.). It binds to 3 receptors: BAFF-R, TACI, and BCMA, all of which are expressed by B cells at various times in their development (Liu and amp; Davidson). BAFF-R signaling activates the NF-kB signaling pathway, and promotes B cell survival, Ig class switching, and antigen presentation (Bossen and amp; Schneider; Liu and amp; Davidson; Naradikian et al.). BAFF also has functions in other cell types: it promotes monocyte survival and activation, proinflammatory cytokine secretion, and differentiation into macrophages (Chang et al.), and co-stimulates anti-CD3-mediated activation of human T cells (Huard et al.; Mackay and amp; Leung).

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

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

Supplier: Serva

Leupeptin hemisulphate