You searched for: Proteins and Peptides

Supplier: STEMCELL Technologies

Interleukin 19 (IL-19) is a member of the IL-10 cytokine family and is produced by keratinocytes, B cells, and monocytes (Romer et al.; Wolk et al.). Expression of IL-19 can be induced by granulocyte-macrophage colony-stimulating factor (GM-CSF) or lipopolysaccharide (LPS; Gallagher et al.). IL-19 is considered to be a proinflammatory cytokine, as it upregulates IL-6 and tumor necrosis factor alpha (TNF-α; Liao et al. 2002). IL-19 binds the IL-20 receptor complex (IL-20R) which comprises IL-20R alpha and IL-20R beta to activate the STAT3 pathway (Dumoutier et al.). IL-19 also induces T-helper cell differentiation towards a Th2 response, resulting in the production of IL-10 and additional IL-19 (Liao et al. 2002; Liao et al. 2004). IL-19 has been implicated in aging, vascular disease, Type I diabetes, and rheumatoid arthritis.

Supplier: STEMCELL Technologies

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).

Supplier: STEMCELL Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf and Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilisation of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways. This product is animal component-free.

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf andamp; Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilisation of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.

Supplier: STEMCELL Technologies

Interleukin 31 (IL-31), a four-helix bundle inflammatory cytokine, belongs to the IL-6 cytokine family which includes IL-6, oncostatin M, leukemia inhibitory factor (LIF), and cardiotrophin-1 ( Dillon et al.). IL-31 signals through a heterodimer composed of IL-31RA (also known as gp130-like receptor or GPL) and the oncostatin-M receptor (OSMR), both of which are expressed on monocytes (Diveu et al.; Ghilardi et al.), epithelial cells (Ip et al.), and keratinocytes (Kato et al.). Signaling through the GPL/OSMR complex activates the JAK/STAT, RAS/ERK, and PI3K/AKT signaling pathways, resulting in the downstream activation of STAT1, STAT3, and STAT5 transcription factors (Cornelissen et al.; Dambacher et al.; Dillon et al.; Ip et al.). IL-31 responses have been associated with allergic responses and inflammatory skin diseases including atopic dermatitis (Cornelissen et al.; Gangemi et al.).

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

R-Spondin-1 (RSPO1) is the prototype member of the R-Spondin (RSPO) protein subfamily of a superfamily of thrombospondin type 1 repeat (TSR-1)-containing proteins (Chen et al.; Kamata et al.; Kazanskaya et al.; Kim et al.). Although unable to initialize signaling, RSPO family members are potent enhancers of WNT signaling (Cruciat and Niehrs; de Lau et al.; Kamata et al.; Kazanskaya et al.). They are characterized by a TSR-1 domain, a carboxy-terminal region with positively charged amino acids, and two N-terminal furin-like cysteine-rich repeats (Glinka et al.; Kazanskaya et al.). R­-Spondin-1 activates β­-catenin signaling via the WNT signaling cascade and by indirectly increasing low-density lipoprotein receptor-related protein 6 (LRP6) on the cell surface. It does this by binding leucine-rich repeat-containing G-protein-coupled receptor 5 (LGR5), and competing with WNT antagonist DKK­1 for binding to the WNT co­receptors, Kremen and LRP­6, which reduces DKK­1-­mediated internalization of LRP6 (Binnerts et al.). RSPO1 is involved in a wide range of pleiotropic roles during embryogenesis, it is required for the specification of hematopoietic stem cells, and it has been shown to be important in the growth, survival, and migration of ovarian cancer cells (Cruciat and Niehrs; de Lau et al.; Genthe and Clements; Liu et al.).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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).

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.

Supplier: STEMCELL Technologies

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).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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-DD promotes growth and survival of renal artery smooth muscle cells and lens epithelial cells, and can act as a macrophage chemoattractant (Changsirikulchai et al.; Lokker et al.; Ray et al.; Uutela et al.).

Supplier: STEMCELL Technologies

Interleukin 13 (IL-13) is a cytokine important in type 2 immune responses and is expressed by T helper type 2 (Th2) cells and group 2 innate lymphoid cells (ILC2s) (Pulendran and Artis). IL-13 binds a receptor composed of IL-4Ra and IL-13Ra1 or IL-13Ra2 (Wynn 2003). IL-13 receptor is expressed on B cells and promotes B cell proliferation, induces class switching to IgG4 and IgE, and functions in the recruitment and activation of IgE-producing B cells (Hershey). The receptor is also expressed on basophils, eosinophils, mast cells, endothelial cells, fibroblasts, monocytes, macrophages, respiratory epithelial cells, and smooth muscle cells (Hershey). Signaling through the IL-13 receptor activates the JAK/STAT and IRS-1/IRS-2 pathways. in vivo, IL-13 has a role in resistance to extracellular helminth parasites by regulating gastrointestinal parasite expulsion, as well as in airway hyperresponsiveness, allergic inflammation, tissue remodeling, tumor cell growth, and fibrosis (Wynn 2015). Secreted IL-13 is a protein consisting of 112 amino acids with a molecular mass of 10 kDa (Hershey). Human IL-13 is not species-specific but has greater activity on human cells compared to mouse cells (Hershey).

Supplier: STEMCELL Technologies

Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to the 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.).

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

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.

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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.).

Supplier: STEMCELL Technologies

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).

Supplier: STEMCELL Technologies

Apolipoprotein H (apo H) has been shown to promote the coagulation of blood platelets by inhibiting thrombomodulin complex and inactivating protein C (Keeling et al.), but can also act as an anticoagulant by binding thrombin and inhibiting its procoagulant effects (Pozzi et al.). Belonging to the lipid-binding apolipoprotein family, within the lipocalin superfamily, apo H is a protein constituent of plasma, with a high affinity for negatively charged phospholipids. The structure of apo H reveals four N-terminal complement control protein (CCP) modules, also known as 'sushi' domains, and a distinct fifth C-terminal domain with four antiparallel beta sheets, two alpha-helices, and an extended loop (Schwarzenbacher et al.). Apo H is the main antigen implicated in antiphospholipid syndrome (APS), an autoimmune condition involving pregnancy complications and vascular thrombosis (Brusch). Studies have also reported that Apo H is involved in the progression of atherosclerosis (Harats and George). 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 ≥93% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.