You searched for: Proteins and Peptides

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Yang et al.; Dorssers et al.; Broughton et al.). IL-3 is produced by activated T cells and has a physiological role in inflammation and allergies by promoting the secretion of inflammatory mediators such as histamine, IL-4, and IL-6 by basophils and eosinophils (Broughton et al.). The IL-3 receptor consists of a unique alpha subunit (CD123) and a beta common subunit (βc or CD131) that is shared with the receptors for IL-5 and GM-CSF, and is the principal signal transduction subunit for these cytokines. IL-3 binding to the heterodimeric receptor activates JAK/STAT, MAPK, and PI3K signaling pathways (Woodcock et al.).

Supplier: STEMCELL Technologies

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).

Supplier: STEMCELL Technologies

Fibroblast growth factor acidic (FGF-acidic), also known as FGF-1, is a potent activator of DNA synthesis, cell proliferation, and chemotaxis and is known to play numerous roles in development, regeneration, and angiogenesis (Jaye et al.; Galzie et al.; Presta et al.). FGF-acidic is produced by multiple cell types and is capable of activating all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It is found in large quantities in the brain, but is also expressed in hepatocytes, vascular smooth muscle cells, neurons of the CNS, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelial cells, and pituitary basophils and acidophils. FGF-acidic is secreted as a disulfide-linked homodimer and is stored in complex with heparan sulfate, a requirement for its interaction with FGF receptors (Guerrini et al.; Mohammadi et al.). Internalized FGF-acidic signals through protein kinase C and promotes cell survival by inhibiting p53 and proapoptotic signaling (Bouleau et al.).

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

Interleukin 6 receptor (IL-6R) alpha is a type I transmembrane glycoprotein that forms a complex with type I transmembrane signal transducer protein gp130 (CD130) and mediates the biological activities of IL-6. IL-6 binds to the membrane-bound non-signaling IL-6R alpha (mIL-6R), and the complex binds to two molecules of gp130 and leads to ‘classical’ IL-6-signal transduction, which includes activation of JAK/STAT, ERK, and PI3K signal transduction pathways (Scheller et al.). In contrast, a soluble form of IL-6R alpha (sIL-6R), which comprises the extracellular portion of the receptor, binds to the secreted IL-6 to form a complex that promotes bioavailability of IL-6. The complex of IL-6 and sIL-6R can bind to gp130 on cells that do not express the IL-6R and are unresponsive to IL-6. This process is known as trans-signaling (Hunter and Jones; Rose-John S). sIL-6R regulates both local and systemic IL-6-mediated events. Elevated levels of sIL-6R have been documented in several disease conditions such as rheumatoid arthritis, myeloma, and Crohn’s disease (Jones et al.; Mihara et al.).

Supplier: STEMCELL Technologies

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

Supplier: STEMCELL Technologies

Trigger a variety of immunological responses with E. coli Lipopolysaccharide O55:B5 (S-form), a lipopolysaccharide (LPS) derived from the O55:B5 serotype of the Gram-negative bacteria and nbsp Escherichia coli. Composed of a lipid A, a core oligosaccharide, and an O antigen, LPS are glycolipid constituents that reside on the outer membranes of gram-negative bacteria (Kitchens RL et al.). LPS protects bacteria against bile salts and lipophilic antibiotics by maintaining the outer integrity of the cell membrane (Bäckhed F et al.). E. coli lipopolysaccharide O55:B5 (S-form), in particular, is predominantly recognized by toll-like receptor 4 (TLR4), which leads to the activation of NF-κβ, a protein complex which plays a key role in regulating immune response (Kuzmich N et al.). Activation of NF-κβ can trigger increased production of pro-inflammatory cytokines IL-1 and TNF-α by macrophages (Matuschak GM et al.). This LPS can also interact with CD14 to activate phospholipase Cγ2 and kinases of the Src family, trigger influxes of extracellular Ca2+, as well as calcineurin-dependent translocation of the nuclear factor of activated T cells (NFAT) family of transcription factors (Li CC et al.). When added to ImmunoCult™-SF macrophage medium (Catalog #10961), stimulation with lipopolysaccharide from E. coli (O55:B5) and IFN-γ supports the polarization to M1 (classically activated) macrophages. Warning: This product is highly pyrogenic. Avoid all means by which the product may enter the bloodstream.

Supplier: STEMCELL Technologies

Platelet-derived growth factor (PDGF) is a dimeric glycoprotein consisting of two disulfide bridge-stabilized polypeptide chains, A and B, which are assembled as heterodimers (PDGF-AB) or homodimers (PDGF-AA and PDGF-BB) (Fretto et al.; Westermark and Heldin). PDGF signals through the receptor tyrosine kinases PDGFRalpha and PDGFRbeta. 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- like 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.). It has been shown that PDGF-AB together with 5-Azacytidine (Catalog #72012), induces the conversion of mature bone and fat cells into tissue-regenerative multipotent stem cells (Chandrakanthan et al.).

Supplier: STEMCELL Technologies

Human Interleukin 4 (IL-4) is important for immune responses to helminth infection as well as in allergic responses (Olpihant et al.). The IL-4 receptor consists of a heterodimer of IL-4Ra and common gamma chain. IL-4 receptor engagement leads to the activation of JAK1/3 and the recruitment of STAT6 and IRS1/2 (Nelms et al.). IL-4 drives immunoglobulin class switching in B cells (to IgE, IgG4), mast cell hyperplasia, mucus production, and the differentiation of naïve T cells into T helper type 2 (Th2) cells, which produce IL-4, IL-5, IL-10, and IL-13 (Bao et al.; Olpihant et al.; Nelms et al.). In addition to Th2 T cells, IL-4 is produced by CD4+ NK T cells, γ/δ T cells, activated basophils, eosinophils, and mast cells. IL-4 consists of 130 amino acids with a predicted molecular weight of 15.1 kDa. Human IL-4 does not cross-react with mouse cells (Park et al.). This product is animal component-free.

Supplier: STEMCELL Technologies

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 regulatory cells, as well as mast cells, NK cells, neutrophils, and regulatory B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the activation of certain immune cells while it promotes the function of B cells, and facilitate healing process. Specifically, this cytokine is important for the function of T regulatory cells as it is a potent suppressor of effector T cell proliferation and cytokine production. Also, IL-10 produced by a subset of macrophages inhibits activation and production of pro-inflammatory cytokines by neighboring macrophages, thus allowing a level of self-regulation. IL-10 enhances B cell proliferation, immunoglobulin secretion, and class II MHC expression (Ouyang et al.).

Supplier: STEMCELL Technologies

Tumor necrosis factor-alpha (TNF-α) is a pro-inflammatory cytokine that activates NF-κB, 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 cancerous cells by stimulating anti-tumor immunosuppressive 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 Hošek). Other effects of TNF-α include vasodilatation and edema formation. In vitro studies of adult rat neural progenitor cells (NPCs) demonstrate that TNF-α reduces neurogenesis in dentate gyrus-derived NPCs, and promotes astrogliogenesis in subventricular zone-derived NPCs (Borsini et al.).

Supplier: STEMCELL Technologies

Fibroblast growth factor 6 (FGF-6) is a heparin-binding member of the FGF family, regulators of cell proliferation, differentiation, and function. FGF-6 binds and signals through the FGF receptors 1c, 2c, and 4 (Ornitz et al.). FGF-6 is a potent mitogen for fibroblasts, vascular endothelial cells, and prostate carcinoma cells (Asada et al.; Pizette et al.; Ropiquet et al.). FGF-6 is primarily expressed in epithelial and mesenchymal cell lineages. During development, FGF-6 is expressed in skeletal muscle, consistent with its role in muscle differentiation and regeneration (Floss et al.). FGF-6 has also been shown to promote chondrogenesis in embryonic somites in conjunction with transforming growth factor beta 2 (TGF-β2; Grass et al.).

Supplier: STEMCELL Technologies

Brain-derived neurotrophic factor (BDNF), like nerve growth factor (NGF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4), is a member of the NGF family of neurotrophins, which are required for the differentiation and survival of specific neuronal subpopulations in both the central and the peripheral nervous systems (Minichiello and Klein; Minichiello et al.). BDNF binds with high affinity to the tropomyosin receptor kinase B (TrkB), and activates AKT and ERK pathways (Mattson et al.). It is expressed in the hippocampus, cortex, and synapses of the basal forebrain. BDNF acts as a survival factor for human embryonic stem cells when plated on either feeder cells or Corning® Matrigel® (Pyle et al.). BDNF regulates synaptic transmission and plasticity at adult synapses in the central nervous system, and contributes to adaptive neuronal responses including long-term potentiation, long-term depression, certain forms of short-term synaptic plasticity, and homeostatic regulation of neuronal excitability (Reichardt). It also has a role in neurogenesis by promoting survival and growth of dorsal root ganglion cells, and hippocampal and cortical neurons (Binder and Scharfman). BDNF, together with glial cell line-derived neurotrophic factor (GDNF) and other supplements, is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Brafman).

Supplier: STEMCELL Technologies

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 (Bartley et al.; de Sauvage et al.; Foster et al.; Sohma et al.). 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 and Kaushansky). The TPO receptor, c-Mpl, is expressed at all stages of megakaryopoiesis, from hematopoietic stem and progenitor cells to mature platelets (Ng et al.).

Supplier: STEMCELL Technologies

Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including 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).

Supplier: STEMCELL Technologies

Macrophage inflammatory protein-1 alpha (MIP-1 alpha), also known as CCL3, is a member of the CC family of chemokines and is most closely related to CCL4 or MIP-1 beta. Mouse MIP-1 alpha signal through CCR1, CCR3, CCR5, and D6 receptors (Menten et al.). MIP-1 alpha exhibits a variety of proinflammatory activities in vitro, including leukocyte chemotaxis, cytokine production, and mast cell activation, and it inhibits the proliferation of hematopoietic stem cells in vitro and in vivo (Cook). MIP-1 alpha plays a critical role in macrophage recruitment into wounds and in tissue repair (DiPietro et al.). It has been demonstrated that blockade of the CCL3/MIP-1 alpha-CCR1 pathway blocks the recruitment of CCR1-expressing CD4+ T cells to the liver, showing a therapeutic potential for treating T cell-mediated liver diseases (Ajuebor et al.).

Supplier: STEMCELL Technologies

Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor and a member of the tumor growth factor (TGF)-beta superfamily. The GDNF family of growth factors also includes neurturin, persephin, and artemin, which have seven conserved cysteine residues called cysteine-knots (Treanor et al.). GDNF family ligands signal through binding to specific GDNF-family receptor-α (GFRα) co-receptors and activate the RET receptor tyrosine kinase (Durbec et al.). Four different forms of GFRα co-receptors have been characterized (GFRα 1-4); GDNF binds specifically to GFRα1 prior to forming a complex with RET (Airaksinen and Saarma). GDNF is known to promote survival and morphological differentiation of midbrain dopaminergic neurons in both in vivo and in vitro studies and increases their high-affinity dopamine uptake (Granholm et al.; Lin et al.). GDNF has also been shown to have restorative effects on dying dopaminergic neurons in response to degenerative toxins (Aoi et al.). GDNF, together with Human Recombinant BDNF (brain-derived neurotrophic factor), BrainPhys™ Neuronal Medium, and other supplements, can be used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Bardy et al.).

Supplier: STEMCELL Technologies

Stem cell factor (SCF) is an early-acting cytokine that plays a pivotal role in the regulation of embryonic and adult hematopoiesis. SCF promotes cell survival, proliferation, differentiation, adhesion, and functional activation of cells at multiple levels of the hematopoietic hierarchy. Together with other cytokines such as thrombopoietin and Flt3/Flk-2 Ligand, SCF is commonly used to promote expansion of primitive hematopoietic stem cells and multi-potent progenitor cells in culture (Martin et al.; Kent et al.). In synergy with various growth factors, including IL-2, IL-3, IL-6, IL-7, G-CSF, and erythropoietin, SCF increases proliferation and differentiation of myeloid and erythroid progenitor cells and a subset of lymphoid progenitor cells (Broudy). SCF is also a primary growth and activation factor for mast cells and eosinophils. SCF exists in two biologically active splice forms: a soluble and a transmembrane isoform. Upon binding to its receptor (c-Kit tyrosine kinase receptor; CD117), it activates PI3K, JAK/STAT, and MAPK pathways. SCF and signaling from c-Kit have also been reported to play an important role in pigmentation, fertility, vasculogenesis, motility of the gut via c-Kit positive interstitial cells of Cajal, and in the migration of neuronal stem and progenitor cells to sites of injury in the brain.

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

Interleukin 1 alpha (IL-1α) is a member of the IL-1 family and a dual-function cytokine. Both the unprocessed precursor and a processed IL-1α protein signal through IL-1 receptor type 1 (IL-1R1). Various cells, including keratinocytes, thymic epithelium, hepatocytes, endothelial cells, fibroblasts, and the epithelial cells of mucous membranes have high levels of intracellular IL-1α precursor, which is also expressed on the surface of monocytes and B lymphocytes (Netea et al.). IL-1α recruits infiltrating cells to a site of injury during necrosis and plays an important role during processes of sterile inflammation (Rider et al.; Cohen et al.). During hypoxia, IL-1α contributes to angiogenesis (Carmi et al.). IL-1α is produced by microglia-like cells after ischemic brain injury, which contributes to the inflammation (Luheshi et al.).

Supplier: STEMCELL Technologies

Mediate calcium phosphate clearance and prevent ectopic calcification with fetuin A, a plasma glycoprotein that forms soluble complexes with calcium and phosphate (Heiss et al.; Price and Lin). Belonging to the cystatin superfamily of cysteine protease inhibitors (Brown and Dziegielewska), fetuin A has also been shown to play a role in lipid transport, acting as a carrier (Kumbla et al.). In cell-based assays, it has been suggested that fetuin A protects against lethal systemic infection through the inhibition of high mobility group box 1 (HMGB1) protein accumulation and release (Li et al.). Fetuin A acts as a natural antagonist against specific TGF-β and BMP signaling proteins, blocking osteogenic differentiation of rat bone marrow cells (Demetriou et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, fetuin A from STEMCELL comes lyophilised with ≥94% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

Supplier: STEMCELL Technologies

Monokine induced by interferon-gamma (MIG), or CXCL9, is a member of the CXC chemokine family. MIG is closely related to two other chemokines: CXCL10 and CXCL11, all of which signal through the CXCR3 receptor (Ding et al.). MIG is secreted by a variety of immune cells including T cells, NK cells, dendritic cells, macrophages, and eosinophils, as well as non-immune cells including hepatic stellate cells, preadipocytes, thyrocytes, endothelial cells, tumor cells, fibroblasts, and glial cells of the central nervous system. MIG has also been shown to act as a chemoattractant for activated T cells and for tumor-infiltrating leukocytes (TILs), but not for neutrophils or for monocytes. MIG has also been reported to be both a tumor suppressor and tumor promoter in various types of cancer.

Supplier: STEMCELL Technologies

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.

Supplier: STEMCELL Technologies

Heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) is a member of the EGF family (Nishi and Klagsbrun). HBEGF promotes blastocyst adhesion to the uterine wall (Iwamoto and Mekada). It also plays a role in smooth muscle cell hyperplasia and brain injury (Nishi and Klagsburn). HBEGF produced by CD4+ T cells promotes wound healing by stimulating migration and proliferation of keratinocytes, fibroblasts, and smooth muscle cells (Blotnick et al.). It binds to EGFR, ErbB4, ErbB2, and ErbB3, activating the PI3K/AKT signaling cascade (Iwamoto and Mekada). HBEGF is produced in a variety of cells, where it contributes to physiological and pathological processes. HBEGF is overexpressed in ovarian, breast, gastric, colorectal, pancreatic, and endometrial cancers, which likely contributes to pathogenesis (Miyata et al.).