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

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.).

Supplier: Anaspec Inc

The Staphylococcus aureus transpeptidase Sortase A (SrtA) anchors virulence and colonization-associated surface proteins to the cell wall. SrtA selectively recognizes a C-terminal LPXTG motif. SrtA readily reacts with its native substrate Abz-LPETG-Dap(DNP)-NH2, cleaving it and catalyzing the formation of an amide bond between the carboxyl group of threonine and the amino group of cell-wall crossbridges. Cleavage of this FRET substrate can be monitored at Ex/Em=320 nm/420 nm.
Sequence:Abz-LPETG-K(Dnp)-NH2
MW:928 Da
% peak area by HPLC:95
Storage condition:-20° C

Supplier: Anaspec Inc

This is a hypoxia-inducible factor-1 (HIF-1 a) 19-mer fragment. HIF-1 functions as master regulator of response to oxygen homeostasis. Hypoxia-induced gene expression is initiated when HIF-1 subunit is stabilized in response to a lack of oxygen. This part of HIF-1 binds to the von Hippel-Lindau factor (VHL) an E3 ubiquitin ligase, and the proline 564 is absolutely critical to the binding process
Sequence:DLDLEMLAPYIPMDDDFQL
MW:2254.6 Da
% peak area by HPLC:95
Storage condition:-20° C

Supplier: STEMCELL Technologies

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.).

Supplier: Anaspec Inc

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases such as cancer, angiogenesis, alopecia, and metastasis. MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region, and C-terminal hemopexin-like domain. It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin, and proteoglycans.

Supplier: Adipogen

FMS-like tyrosine kinase 3 ligand (FLT3L) acts as a growth factor that increases the number of immune cells (lymphocytes (B cells and T cells)) by activating the hematopoietic progenitors. It binds to FLT3 (CD135) which is found on multipotent progenitor (MPP) and common lymphoid progenitor (CLP) cells in mice. FLT3L induces the mobilization of the hematopoietic progenitors and stem cells in vivo which may help the system to kill cancer cells. FLT3L is crucial for steady-state pDC (plasmacytoid dendritic cells) and cDC (classical dendritic cells) development. Deficiency of FLT3L causes a dramatic decrease in DC numbers, whereas increasing its availability increase in DC numbers.

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

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.). This product is animal component-free.

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: Anaspec Inc

This GLP-1 (7-36)amide contains an additional Lysine (K) residue at its N-terminus, with Biotin coupled to the Lysine side chain. GLP-1 (7-36) amide is an incretin hormone that causes glucose dependent release of insulin by pancreatic beta cells. It is the cleavage product of GLP-1 (1-36) amide peptide (Cat# AS-22460). Both GLP-1 (7-36) and GLP-1 (7-37) - Cat# AS-20761, also play roles in gastric motility (gastric emptying), on the suppression of plasma glucagon levels (glucose production) and possibly on the promotion of satiety and stimulation of glucose disposal in peripheral tissues independent of the actions of insulin. GLP-1 (7-36) has a short half life of less than 2 minutes, and like GIP, is rapidly degraded by the enzyme dipeptidyl peptidase IV (DPP-4), which is widely expressed in a number of sites, including the endothelial cells of small gut arterioles. DPP-4 degrades GLP-1 (7-36) into the non insulinotropic GLP-1 (9-36) - Cat# AS-65070 (some studies suggest it may have weak insulinotropic activity). As a result, the majority of GLP-1 (and GIP) is inactivated as an insulinotrope before reaching the systemic circulation.
Sequence: HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRK(Biotin)-NH2
MW: 3551.8 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Supplier: Adipogen

Interleukin-4 (IL-4) is a cytokine produced by type 2 helper T cells, the Th2 cells. These cells tends to make a specific set of lymphokines including IL-4, IL-5, IL-6, IL-10, IL-13, IL-3 and GM-CSF and fail to produce IL-2, IFN-gamma, and lymphotoxin (TNF-beta). In addition, mast cells can produce IL-4. IL-4 exerts numerous effects on various hematopoietic cell types. On B cells, IL-4 promotes immunoglobulin class switching to IgE and IgG1 isotypes and upregulates MHC class II and CD23 expression. IL-4 promotes survival, growth and differentiation of both T and B lymphocytes, mast cells and endothelial cells. In addition, IL-4 inhibits the production of TNF, IL-1 and IL-6 by macrophages.

Supplier: Anaspec Inc

Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptides is a highly soluble fluorogenic MMP substrate for MMP-2, 8, 12, 13 and 14, containing the MMP cleavable Gly-Leu bond and EDANS/DABCYL. Fluorogenic assays using TNO211 are sensitive and can detect MMP activity in culture medium from endothelial cells and untreated synovial fluid from patients. Abs/Em = 340/490 nm.
Sequence:DABCYL-(γ-Abu)-PQGL-E(EDANS)AK-NH2
MW:1326.5 Da
% peak area by HPLC:95
Storage condition:-20° C

Supplier: STEMCELL Technologies

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.

Supplier: Anaspec Inc

The intrastriatal perfusion with the neurotensin(1-13) [NT(1-13)] and its active fragment NT(8-13) on striatopallidal GABA leads to the increased striatal and pallidal GABA release, and this effect is antagonized by intrastriatal perfusion with the NT receptor antagonist. Neurotensin(8-13) is as potent as neurotensin but ineffective in [D-Tyr(11)]neurotensin. In the caudal nucleus accumbens, neurotensin(8-13) and neurotensin appears more potent than [D-Tyr(11)]neurotensin. In contrast, in the rostral nucleus accumbens, neurotensin(8-13) is less potent than [D-Tyr(11)]neurotensin and neurotensin.
Sequence:RRPYIL
MW:817 Da
%Peak area by HPLC:≥95%
Storage condition: -20°C

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 regulatory T 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 STAT5-dependent proliferation and survival in vitro (Clark et al.; Corfe and Paige). 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: Adipogen

Neuregulin-4 (Nrg4) belongs to a small family of EGF-like (EGFL) domain-containing proteins that are synthesized as transmembrane precursors and undergo proteolytic cleavage. The EGF-like domain (aa 5-46) of Nrg4 (aa 1-53) directly binds to the receptors ErbB3 and 4. Nrg4 is a cold induced adipokine, highly expressed in adipose tissues and enriched in brown fat. It is increased during brown adipocyte differentiation and reduced in rodent and human obesity. It promotes neurite outgrowth and protects against diet-induced insulin resistance and hepatic steatosis through attenuating hepatic lipogenic signaling. This hepatic effect of Nrg4 is mediated by ErbB3 and ErbB4 signaling that negatively regulates de novo lipogenesis mediated by LXR and SREBP1c. This effect of Nrg4 on fatty liver and insulin resistance could lead to the development of Nrg4 as an effective therapeutic biological for the treatment of NAFLD and type 2 diabetes. GST-Nrg4 (aa 1-53) recombinant protein has been shown to mimic the effect of endogenous secreted Nrg4 on liver lipogenesis.

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 lyophilized with ≥ 93% purity.

Supplier: Adipogen

Nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) catalyzes the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form nicotinic acid mononucleotide (NaMN) as a substrate but with lower efficiency. NMNAT2 also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. It is highly expressed in brain, in particular in cerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and putamen. NMNAT2 is also found in the heart, skeletal muscle, pancreas and islets of Langerhans. NMNAT2 is essential for axon growth and survival. Its loss from injured axons may activate Wallerian degeneration (axon degeneration induced by nerve injury), whereas NMNAT overexpression rescues axons from degeneration.

Supplier: STEMCELL Technologies

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).

Supplier: Anaspec Inc

Like human Gastrin-1 “Little Gastrin,” rat Gastrin-1 “Little Gastrin” contains 17 amino acids, but differs from human Gastrin by 3 amino acids at the C-terminus. Secretion of Gastrin is induced by food intake and causes the release of gastric acid. Synthesized by the G cells in the gastric mucosa, it is one of the major bioactive forms of Gastrin (the other bioactive form is Gastrin-34). Both Gastrin-17 and Gastrin-34 are carboxy-amidated and partially tyrosine sulfated. Binding of Gastrin to the CCK2/gastrin receptor requires carboxy-amidation, however sulfation is not necessary for binding to the receptor.
Sequence: Pyr-RPPMEEEEEAYGWMDF-NH2
MW: 2126.3 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Supplier: STEMCELL Technologies

Interleukin 1 beta (IL-1β) is synthesized 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

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 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.).

Supplier: Anaspec Inc

Myelin oligodendrocyte glycoprotein (MOG) is a member of the immunoglobulin superfamily and is expressed exclusively in the central nervous system. It is a glycoprotein observed to be important in the myelination of nerves. It is a central molecule actively studied for its role in Multiple Sclerosis. MOG (35-55) is able to induce autoantibody production and relapsing-remitting neurological disease causing extensive plaque-like demyelination. Autoantibody response to MOG (35-55) has been observed in multiple sclerosis (MS) patients and MOG (35-55)-induced experimental autoimmune encephalomyelitis (EAE) C57/BL6 mice and Lewis rats.
Sequence: MEVGWYRSPFSRVVHLYRNGK
MW: 2582 Da
% Peak Area by HPLC: ≥ 95%
Storage condition: -20°C

Supplier: Anaspec Inc

Renin, a highly specific aspartyl protease, cleaves angiotensinogen, produced in the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE (Angiotensin Converting Enzyme). Angiotensin II constricts blood vessels, leading to increased blood pressure. It also increases the secretion of ADH and aldosterone, and stimulates the hypothalamus to activate the thirst reflex. Since an overactive renin-angiotensin system leads to hypertension, renin is proposed as a therapeutic target for this disease.

Recombinant rat pro-renin was expressed in HEK cells. Purified enzyme was converted to the active renin by tryptic activation followed by removal of trypsin. The molecular mass of active rat renin is approximately 40 kDa. The activity of enzyme can be measured in FRET-based assays

Supplier: Anaspec Inc

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-12 (macrophage elastase) is involved in smoke-induced emphysema, tumor and other diseases. MMP-12 is secreted as a 54-kDa zymogen and becomes the mature 45-kDa active form after proteolytic cleavage. MMP-12 has a broad range of substrates, including α-1 proteinase inhibitor, α-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.

The sequence (Accession # NP_002417) corresponding to the catalytic domain (aa 106-267) of Human MMP-12 was expressed in E. coli. The recombinant human MMP-12 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-12 Catalytic Domain is 18 kDa.

Supplier: STEMCELL Technologies

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.

Supplier: Adipogen

Interleukin-18 (IL-18) is a costimulatory factor for production of interferon-gamma (IFN-gamma) in response to toxic shock and shares functional similarities with IL-12. IL-18 is synthesized as a precursor 24kDa molecule without a signal peptide and must be cleaved to produce an active molecule. IL-1 converting enzyme (ICE; Caspase-1) cleaves pro-IL-18 at aspartic acid in the P1 position, producing the mature, bioactive peptide that is readily released from the cells. It is reported that IL-18 is produced from Kupffer cells, activated macrophages, keratinocytes, intestinal epithelial cells, osteoblasts, adrenal cortex cells and murine diencephalon. IFN-gamma is produced by activated T or NK cells and plays critical roles in the defense against microbiral pathogens. IFN-gamma activates macrophages and enhances NK activity and B cell maturation, proliferation and Ig secretion. IFN-gamma also induces expression of MHC class I and II antigens and inhibits osteoclast activation. IL-18 acts on T helper type-1 (Th1) T cells and in combination with IL-12 strongly induces them to produce IFN-gamma. Pleiotropic effects of IL-18 have also been reported, such as enhancement production of IFN-gamma and GM-CSF in peripheral blood mononuclear cells, production of Th1 cytokines, IL-2, GM-CSF, IFN-gamma in T cells and enhancement of Fas ligand expression by Th1 cells.