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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 (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.).

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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.).

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Interleukin 10 (IL-10) is the founding member of the IL-10 family of class II cytokines. All of the IL-10 cytokine family members have a four-helix bundle consisting of α-helical folds. Upon binding to its receptor, IL-10 activates signaling through JAK1 and STAT3. It is produced by dendritic cells, macrophages, and CD4+ T cells, as well as mast cells, NK cells, neutrophils, and B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the expression of pro-inflammatory cytokines and promote healing processes, and is important for the function of 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.).

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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.).

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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.).

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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.

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Sonic hedgehog (Shh) is a member of the Hedgehog family of secreted signaling proteins that has a prominent role in patterning during early mammalian development (Ho and Scott). It is expressed during early embryogenesis in a variety of tissues (Finco et al.). During patterning of the central nervous system, Shh directly acts on cells to specify neural cell fates, regulates proliferation and survival of oligodendrocyte precursors and neural crest cells and stimulates proliferation, differentiation, and axon growth (Ho and Scott; Martí). Shh also regulates T cell differentiation and activation (Crompton et al.). Recombinant Mouse Shh is a fully biologically active molecule.

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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.

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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.).

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Dickkopf-related protein 1 (DKK-1) is a member of the Dickkopf family and is a secreted protein that inhibits the canonical WNT pathway by competitive binding to low-density lipoprotein receptors (LRP)-5 and 6 with high affinity, thereby decreasing β-catenin protein stability (Niehrs). DKK-1 regulates embryonic development and contains two conserved cysteine-rich domains separated by a linker region and an N-terminal signal peptide (Krupnik et al.; Lieven et al.). A family of human DKK-related genes composed of DKK-1, DKK-2, DKK-3, and DKK-4 have been characterized together with a unique DKK-3 related protein termed Soggy (Krupnik et al.). DKK-1 has been shown to support the generation of myeloid-derived suppressor cells (MDSCs) and thus is a negative regulator of antitumor immune responses (D’Amico et al.). DKK-1 from thrombocytes is an important regulator of leukocyte infiltration and induces Th2 cell polarization and potentiates Th2 cell cytokine expression (Chae et al.). DKK-1 has also been shown to drive cardiac and retinal differentiation from induced pluripotent stem (iPS) cells (Lian et al.). Protein contains a His-residue tag at the carboxyl end of the polypeptide chain.

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

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Fractalkine (CX3CL1) is a unique chemokine belonging to the CX3C family, and is characterized by a C-X3-C cysteine motif within the chemokine domain, near the amino terminus of the protein (Bazan et al.). The chemokine domain is connected to an extended mucin-like stalk, followed by a transmembrane region, and a C-terminal intracellular domain (Imai et al.; Jones et al.). The protein signals through interaction with a single receptor, CX3CR1, expressed on monocytes, natural killer cells, T cells, microglia, and smooth muscle cells. Fractalkine is upregulated in endothelial cells by inflammatory signals and is synthesized as a membrane-bound molecule that mediates cell migration and adhesion (White and Greaves). Cleavage at the base of the stalk by metalloproteinases generates a soluble chemokine, which functions as a potent chemoattractant of target cells (Garton et al.; Apostolakis and Spandidos). Fractalkine has been implicated in pathology of inflammatory diseases, such as atherosclerosis and other vascular diseases, and has anti-apoptotic functions (White and Greaves).

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Basic fibroblast growth factor (bFGF) is a prototypic member of the fibroblast growth factor family. Cytokines in the FGF family possess broad mitogenic and cell survival activities (Folkman and Klagsbrun; Kimelman and Kirschner) and are involved in a variety of biological processes including cell proliferation, differentiation, survival, and apoptosis (Folkman and Klagsbrun; Klagsbrun; Rifkin and Moscatelli). bFGF has the β-trefoil structure (Ponting and Russell), binds to the four FGF receptor (FGFR) family members, and activates JAK/STAT, PI3K, ERK1/2, and other receptor tyrosine kinase (RTK) signaling pathways. It supports the maintenance of undifferentiated human pluripotent stem cells (Xu et al.; Kang et al.), stimulates human pluripotent stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.). This version of bFGF is the full-length bFGF protein encoded by the human FGF2 gene consisting of 154 amino acid residues. This product is animal component-free.

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Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to a heterotrimeric receptor consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). Targeted deletions of the IL-2 gene in mice resulted in development of autoimmune hemolytic anemia, followed by ulcerative colitis. Similar effects were observed in mice that were deficient in IL-2 receptor α (Gaffen and Liu).

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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. The precursor 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 (Cohen et al.; Rider et al.). During hypoxia, IL-1α contributes to angiogenesis (Carmi et al.). Studies in mice show that IL-1α is produced by microglia-like cells after ischemic brain injury, which contributes to the inflammation (Luheshi et al.).

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Fibroblast growth factor 18 (FGF-18) is a growth factor and member of the FGF subfamily. FGF-18 is most similar to FGF-8 and FGF-17, and is secreted in adult lung and developing tissues (Ohbayashi et al.). FGF-18 signals through FGF receptor 3 (FGFR3) to regulate proliferation, differentiation, and matrix production of articular and growth plate chondrocytes in vivo and in vitro (Davidson et al.). FGF-18 has skeletal functions and protects articular cartilage by gene expression profiling and regulates proliferation and differentiation of midline cerebellar structures (Mori et al.). Also, recombinant human FGF-18 has been shown to effectively regulate hair growth (Song et al.).

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GRO (growth-regulated oncogene)-beta or CXCL2 is a member of the CXC family, which plays an integral role in recruitment and activation of neutrophils and basophils in response to tissue injury and microbial infection. GRO-beta and GRO-gamma are closely related to GRO-alpha and share 90% and 86% amino acid sequence homology, respectively, with GRO-alpha. Receptor-binding studies have demonstrated that GRO-alpha, -beta, and -gamma signal mainly through G protein-coupled receptors CXCR1 and CXCR2 (Ahuja and Murphy). GRO-beta is expressed in epithelial cells, monocytes, fibroblasts, and melanocytes and is further induced during inflammatory, epithelialization, and angiogenic processes, for example during the wound healing process of human burn wounds (Zaja-Milatovic and Richmond). GRO-beta also stimulates mitogenesis in certain human melanoma cells (Unemori et al.).

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

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Tumor necrosis factor-α (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 cancer cells in vitro 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 andamp; Hosek). Other effects of TNF-α include vasodilatation and edema formation.

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Epidermal growth factor (EGF) is the founding member of the EGF family of proteins and is characterized by high affinity binding to various EGF receptors (EGFRs) and the production of mitogenic responses (Carpenter and Cohen). EGF promotes EGFR dimerization, resulting in activation of downstream pathways including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signaling. EGF is secreted by the gut-associated salivary and Brunner’s glands, is found in a variety of body fluids, and stimulates cell proliferation and differentiation in rodent and neonatal human intestine (Wright et al.). EGF can stimulate the proliferation of mouse embryonic stem cells or induce the terminal differentiation/growth inhibition of A431 cells (Heo et al.).

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Commonly known as vaspin, Serpin A12 is an adipokine that is thought to perform insulin-sensitizing functions, such as the regulation of kallikrein 7 (KLK7), an insulin-inhibiting protease (Heiker et al.). The Serpin A12 glycoprotein belongs to the serine protease inhibitor family (serpin), and is mainly associated with obesity, insulin resistance, and glucose metabolism, but may also protect against high fat-induced bone loss (Wang et al.). Serpins share a highly conserved core structure with multiple α-helices, β-strands, and a reactive site loop (RCL) to interact with the target protease (Huntington). It is expressed predominantly in visceral adipose tissue and at significantly higher amounts in obese individuals (Kurowska et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, Serpin A12 from STEMCELL comes lyophilised with ≥94% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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Use angiopoietin-like protein 2 (ANGPTL2) to regulate tissue remodeling through integrin α5β signaling and activation of p38 mitogen-activated protein kinases (MAPK) (Odagiri et al.; Tabata et al.). Highly expressed in the heart, small intestine, and stomach, ANGPTL2 is a glycosylated secretory protein that contains a coiled domain and a fibrinogen-like domain (Kim et al.). Studies have shown that the coiled-coil domain of ANGPTL2 functions as a growth factor, enhancing the survival of hematopoietic stem cells (HSCs) ex vivo (Broxmeyer et al.). ANGPTL2 is also known to play a role in obesity and metabolic diseases, promoting local inflammation in adipose tissue and systemic insulin resistance in mice models (Tabata et al.). By activating an inflammatory cascade in endothelial cells and increasing macrophage infiltration, ANGPTL2 accelerates vascular inflammation which may lead to endothelial dysfunction and atherosclerosis progression (Horio 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, sclerostin from STEMCELL comes lyophilised with ≥92% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Neurotrophin-4 (NT-4) is a member of the nerve growth factor family which includes neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and nerve growth factor (NGF), all of which promote the differentiation, growth, and survival of peripheral and central nervous system neurons (Eide et al.). NT-4 binds and activates tropomyosin receptor kinase B (TrkB) at the cell surface; in doing so, it acts as a survival factor for certain populations of sensory neurons (Berkemeier et al.; Skaper). It has been shown that NT-4, together with BDNF, promotes neurite extension and maturation, as well as maintenance of differentiated cerebellar granule cells (Gao et al.).

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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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 Th2 cells, which produce IL-4, IL-5, IL-10, and IL-13 (Bao et al.; Nelms et al.; Olpihant et al.). In addition to Th2 cells, IL-4 is produced by CD4+ NK T cells, γ/δ T cells, activated basophils, eosinophils, and mast cells. Human IL-4 does not cross-react with mouse cells (Park et al.).

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Epidermal growth factor (EGF) is characterized by high-affinity binding to various EGF receptors (EGFRs) and the production of mitogenic responses (Carpenter and Cohen). EGF promotes EGFR dimerization, resulting in activation of downstream pathways including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signaling. EGF is secreted by the gut-associated salivary and Brunner’s glands, is found in a variety of body fluids, and stimulates cell proliferation and differentiation in rodent and neonatal human intestine (Wright et al.). Central nervous system stem cells also proliferate in response to the EGF stimulus (Reynolds and Weiss). This product is animal component-free.

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Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to ST2 receptor and activates NF-κB 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, 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.).

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

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Oncostatin M (OSM) is a member of interleukin 6 (IL-6) family of cytokines and bears close resemblance to leukemia-inhibitory factor (LIF) and granulocyte colony-stimulating factor (G-CSF) in amino acid sequence and its modulation of differentiation in a variety of cell types (Rose and Bruce). OSM signals through type I receptor (consisting of gp130 and LIF receptor (LIFR)) and type II receptor (consisting of gp130 and OSM receptor (OSMR)), which eventually activate the JAK/STAT pathway (Auguste et al.; Gómez-Lechón). OSM is primarily produced by activated T cells and monocytes, and also by activated macrophages, neutrophils, mast cells, and dendritic cells. OSM is also produced within the bone microenvironment by cells of both hematopoietic and mesenchymal origin including osteocytes and osteoblasts. OSM is involved in differentiation, cell proliferation, hematopoiesis, and inflammation, and also has been shown to have implications in liver development, bone formation and resorption (Sims and Quinn; Tanaka and Miyajima).

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Interleukin 6 (IL-6) is a pleiotropic growth factor with the 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 (Hirano 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 JAK/STAT signaling pathway (Mihara et al.; Peters et al.; Tanaka et al.). This product is animal component-free.