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

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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.

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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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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).

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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 (Galzie et al.; Jaye 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 central nervous system, 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 via protein kinase C and promotes cell survival by inhibiting p53 and proapoptotic signaling (Bouleau 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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Receptor activator of nuclear factor kappa-B ligand (RANKL) is a member of the tumor necrosis factor (TNF) superfamily (Anderson et al.). Cytokines in the TNF superfamily are involved in a variety of long-term cellular activities such as differentiation, proliferation, and cell death (MacEwan). RANKL is a type II homotrimeric transmembrane protein expressed in both a membrane-bound and secreted form (Ikeda et al.). RANKL binds to the receptor activator of nuclear factor kappa-B (RANK). Upon binding to its receptor, RANKL activates the AKT signaling pathway (Moon et al.). Osteoprotegerin (OPG) may also bind RANKL, and this binding competes with RANKL-RANK binding (Lacey et al.). RANKL is involved in osteoclastogenesis (Lacey et al.; Yasuda et al.) and T cell activation (Wong et al.). 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 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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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 embryonic stem cells (Xu et al.; Kang et al.), stimulates human embryonic stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.).

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Thymus-expressed chemokine (TECK), or CCL25, is a member of the CC family of chemokines that regulates the movement of lymphocytes in the thymus and in the small intestine. TECK induces chemoattraction by binding the chemokine receptor CCR9, which is expressed on immature pre-T cells and thymocytes (Youn et al.; Uehara et al.). In the thymus, TECK is produced by stromal cells, whereas in the small intestine TECK is primarily produced by epithelial cells (Vicari et al.; Bowman et al.; Kunkel et al.). CCR9 is a G protein-coupled receptor and is expressed on most thymocytes, but not on natural killer cells, monocytes, eosinophils, basophils, and neutrophils (Wu et al). In Jurkat cells, binding of TECK to CCL9 has been shown to increase levels of intracellular calcium (Cheng-Rong et al). TECK/CCR9 signaling has also been linked to many cancers, as these molecules have been shown to mediate anti-apoptotic processes by activating the PI3K/AKT signaling pathway, weakening the effect of cytotoxic T cells by regulating STAT signaling. Additionally, TECK induces metastasis by increasing the expression of MMP2 and MMP9 (Tu et al.).

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Interleukin 6 (IL-6) is a pleiotropic growth factor with a 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 (Nordan et al.; Van Snick et al.; Gauldie 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 the JAK/STAT signaling pathway (Mihara et al.; Peters et al; Tanaka et al.).

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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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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.).

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Insulin-like growth factor 1 (IGF-I) is a polypeptide that belongs to the family of insulin-like growth factors that are similar in molecular structure to proinsulin. IGF-I binds to the IGF-I receptor and is a potent activator of the PI3K/AKT pathway and also activates ERK1/2 signaling. IGF-I is required for embryonic development, and it is produced mainly in the liver in response to a hepatocyte growth hormone. In the absence of insulin, IGF-I is necessary for the maintenance of human pluripotent stem cells (Wang et al.). Together with IL-3, IGF-I stimulates differentiation and proliferation of myeloid cells and has been shown to regulate lymphopoiesis by stimulating proliferation and differentiation of T and B cells in lymphoid organs (Heemskerk et al.).

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Monocyte chemotactic protein-1 (MCP-1), also known as CCL2, is a member of the CC family of chemokines. The protein is primarily induced by platelet-derived growth factor (PDGF) gene (Cochran et al.). The biological effects of MCP-1 are mediated via the specific G-protein-coupled receptor CCR2 which in turn activates signal transduction pathways leading to monocyte transmigration (Sozzani et al.). Migration of monocytes from the bloodstream across the vascular endothelium is required for routine immunological surveillance of tissues, as well as other immunomodulatory effects. MCP-1 is produced by a variety of cell types, including fibroblasts and endothelial, epithelial, smooth muscle, mesangial, astrocytic, monocytic, and microglial cells, which are important for antiviral responses in the peripheral circulations and in tissues (Cushing et al.; Deshmane et al.). MCP-1 plays a role in physiological processes such as neurogenesis, neuroprotection, and neurotransmission and has important implications in neurological disorders such as multiple sclerosis and Alzheimer’s disease, in which it is produced during neuroinflammation at the sites of lesions (Conductier et al.).

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SARS-CoV-2 Recombinant Spike Protein, aa16-685 is expressed in HEK293 cells and is one of four structural proteins encoded by the SARS-CoV-2 genome. The Spike Protein plays a key role in attachment to host cells, allowing invasion through clathrin-mediated endocytosis. The Spike Protein can be cleaved by host cell proteases after aa685 to yield the N-terminal S1 subunit and C-terminal S2 region. The S1 subunit is responsible for interacting with the host cell receptor (angiotensin-converting enzyme II) through a receptor-binding domain that is highly conserved with SARS-CoV. The S1 subunit has two conformations: a ‘down’ conformation in which the receptor is inaccessible, and an ‘up’ conformation in which the receptor is accessible. These conformational changes are key for monoclonal antibody drugs and vaccine development. SARS-CoV-2 Recombinant Spike Protein contains a polyhistidine tag at the amino terminus; it also contains a FLAG tag at the carboxy terminus.

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Bone morphogenetic protein 2 (BMP-2) is a member of the transforming growth factor beta (TGF-β) superfamily. BMP-2 is a disulfide-linked homodimer, acts as a ligand for complexes of type I and II BMP receptors, and primarily activates SMAD1/5/8 signaling (Nohe et al.). BMP-2 is a potent differentiation factor and directs human pluripotent stem cells (hPSCs) towards various cell types including extra-embryonic endoderm, mesenchymal cells, and chondrocytes (Pera et al.). Although BMP-2 expression is low in healthy cartilage, its expression is upregulated at the site of cartilage damage (Blaney Davidson et al.). BMP-2 induces bone and cartilage formation in vitro and is able to induce chondrogenesis in human mesenchymal stem cells (Schmitt et al.). This product is animal component-free.

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RANTES (regulated upon activation, normal T cell expressed and secreted), also known as CCL5, is a member of the CC family of chemokines and is able to recruit leukocytes to sites of inflammation (Schall et al.). RANTES is secreted by T lymphocytes, macrophages, platelets, synovial fibroblasts, tubular epithelium, and certain types of tumor cells (Aldinucci and Colombatti; Soria and Ben-Baruch). This chemokine exerts its effect by interacting with the chemokine receptors CCR1, CCR3, CCR4, and CCR5. RANTES plays an active role in recruiting a variety of leukocytes into inflammatory sites, including T cells, macrophages, eosinophils, and basophils. In collaboration with certain cytokines that are released by T cells such as IL-2 and IFN-γ, RANTES also induces the activation and proliferation of NK cells to generate CC chemokine-activated killer cells, which are highly cytolytic (Lv et al.; Maghazachi et al.). It has been shown that RANTES produced by CD8+ T cells inhibits HIV infection of primary human peripheral blood mononuclear cells (Appay and Rowland-Jones; Cocchi et al.).

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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 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). FGF-8B signals through FGF receptors (FGFRs) to activate PI3K and MAPK pathways. FGF-8B regulates gastrulation, epithelial-mesenchymal transition, and mesenchymal to epithelial differentiation during embryonic development. FGF-8B has also been found in peripheral blood leukocytes and healthy bone marrow samples (Mattila and 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 testes (Valve et al.). 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.). This product is animal component-free.

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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 (IL-7R) 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). Although a deficiency in IL-7R still permits the generation of normal numbers of peripheral B cells in humans, stimulation of human B cell precursors with IL-7 could promote STAT-5-dependent proliferation and survival in vitro (Clark et al.; Corfe and Paige).

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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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A type 1 membrane glycoprotein belonging to the immunoglobulin superfamily, cluster of differentiation 200 (CD200) binds the CD200 receptor (CD200R) that is expressed on the surface of myeloid cells and T cells (Wright et al.), and has been shown to inhibit myeloid cell activity and macrophage cytokine production (Jenmalm et al.). Homologues of CD200 have been identified in viruses and can interact with CD200R to reduce macrophage pro-inflammatory cytokine production (Foster-Cuevas et al.). Studies have shown that the immunosuppressive effects of CD200 can promote acceptance of allogeneic tissue grafts in hosts (Gorczynski et al.), whereas dysregulation of CD200/CD200R can contribute to the development of autoimmune conditions, such as rheumatoid arthritis (Ren et al.). CD200 contains two immunoglobulin-like domains, a V-type domain and a smaller C2-type domain (Hatherley et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, cluster of differentiation 200 from STEMCELL comes lyophilised with ≥95% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein. Human recombinant CD200 at 2 μg/ml can bind human CD200R (His and hFc tag) with a linear range of 5 to 28 ng/ml, as determined by functional ELISA.

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Prolactin is a peptide hormone of pituitary origin and is well known for the stimulation, initiation, and maintenance of lactation. Prolactin is also known to regulate mammary gland development and immune system, and has an essential role in metabolism and behavioral modification (Bernichtein et al.). Prolactin actions are mediated by the prolactin receptor (PRLR), which is a single-chain transmembrane protein composed of an extracellular, transmembrane, and intracellular domain. It has also been indicated that high to normal circulating levels of prolactin increase breast cancer risk, and dopamine agonists have been suggested to be effective for treatment (Bernichtein et al.). Prolactin levels have been reported to be higher in multiple sclerosis patients, which promotes B cell autoreactivity (Correale et al.). It has been shown that administration of recombinant prolactin after bone marrow transplantation in mice promotes immune and myeloid reconstitution (Sun et al.).

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Use Interleukin 37 (IL-37) to inhibit the expression of inflammatory cytokines, such as IL-6, MIP-1α, MIP-1β, and TNF-α, in a MAPK-dependent manner (Qi et al.). A secreted protein belonging to the interleukin-1 cytokine family, IL-37 acts as an anti-inflammatory alarmin, with predominant expression in monocytes, and constitutive secretion by myeloid dendritic cells (Rudloff et al.). IL-37 has been shown to limit inflammation in human blood M1 macrophages by binding to extracellular surface receptors, requiring IL-1R8 as a coreceptor (Li et al.). It also has protective effects against obesity-induced inflammation and insulin resistance, reducing adipogenesis and activating AMPK signaling both in vitro and in vivo (Ballak et al.). In humans, the IL-37 gene undergoes alternative splicing, resulting in multiple isoforms of the protein (Boraschi et al.). For consistency and reproducibility across your applications, Interleukin 37 from STEMCELL comes lyophilised with ≥93% purity.

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TRAIL (TNF-related apoptosis-inducing ligand) belongs to the tumor necrosis factor (TNF) superfamily and is associated with initiating apoptosis. TRAIL has four major receptors: two death receptors DR4 and DR5, and two decoy receptors DcR1 and DcR2. TRAIL binds to the death receptors, which recruits the Fas-associated death domain (FADD) and activates caspases 8 and 10, which eventually leads to apoptosis (Pitti et al.; Wiley et al.; Zauli and Secchiero). It has been shown that mice lacking the expression of TRAIL have defects in thymocyte apoptosis and negative selection, and these mice had increased susceptibility to autoimmune diseases (Lamhamedi-Cherradi et al.).

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Chemokine ligand 19 (CCL19), also known as macrophage inflammatory protein-3 beta (MIP-3β), is a member of the CC chemokine family, which plays key roles in inflammatory responses, T cell activation, homeostasis, and development (Yan et al.). CCL19 is expressed in lymph nodes, thymus, and activated bone marrow stromal cells; it binds to C-C motif chemokine receptor 7 (CCR7) to induce migration of macrophages, T cells, and B cells (Gibejova et al.). Clinically, the expression of CCL19 is correlated to autoimmune diseases such as rheumatoid arthritis and cancer (Pickens et al.; Zhang et al.).

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Growth differentiation factor 5 (GDF-5) is a member of the bone morphogenetic protein (BMP) subclass of the transforming growth factor beta (TGF-β) superfamily. It binds a receptor complex comprising BMPR1B and BMPR2, which then activates the SMAD signaling pathway (Carreira et al.; Nishitoh et al.; Osório et al.). GDF-5 enhances chondrogenic differentiation of mesenchymal stem cells, skeletogenesis, and dendrite growth during development (Coleman et al.; Francis-West et al.). Studies in rat demonstrated that GDF-5 regulates patterning, neurogenesis, astrogliogenesis, and neuronal specification (Gajavelli et al.; Krieglstein et al.; O’Keeffe et al.).

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Transforming growth factor (TGF) beta 2 is a member of the TGF-β superfamily and regulates diverse cellular phenotypes. Similar to TGF-β1 and -β3, TGF-β2 signals via serine-threonine kinase type I and II receptors and activates signal transduction via SMAD family proteins, regulating a variety of functions such as cell proliferation, differentiation, wound healing, apoptosis, and metabolism (de Caestecker; Massague; Zuniga et al.). TGF-β2 is important in many developmental processes; for example, mice with TGF-β2 deletions show defects in the development of cardiac, lung, craniofacial, limb, eye, ear, and urogenital systems (Dunker and Kreiglstein).