You searched for: Proteins and Peptides

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Interleukin 5 (IL-5) is a member of the short-chain 4-α-helical bundle subset of hematopoietic cytokines. It binds to a receptor consisting of IL-5Ra, which is specific for IL-5R, and common beta chain, which is shared with the receptor for IL-3 and GM-CSF (Shearer). Upon binding to its receptor, IL-5 activates the JAK/STAT and MAPK pathways. IL-5 is produced by Th2 cells, eosinophils, and activated mast cells. It functions in the recruitment, activation, proliferation, and survival of eosinophils, thus playing an important role in allergic inflammation, asthma, and parasite immunity. Stimulation of eosinophils with IL-5 leads to their activation, upregulation of CD11b expression, and inhibition of apoptosis (Shearer).

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Interferon-alpha (IFN-α) is a type I interferon, produced by virus infected cells, and is released as a soluble factor to initiate antiviral responses (Isaacs and Lindenmann). IFN-α2 is the most potent IFN-α used in fundamental research and in most clinical applications. The best known IFN-α2 subvariants, 2A and 2B, differ by only one or two amino acids at positions 23 and/or 34 of the mature protein (von Gabain et al.). Type I IFNs exert potent antitumor activity by increasing the cytotoxic activity of NK and T cells, as well as inhibiting the proliferation of cancer cells (Paul et al.). Additionally, it has been shown that proinflammatory IFN-α modulates the function of B cells in patients with systemic lupus erythematosus (Chang et al.) and pegylated form of IFN-α 2A and 2B has implications in the treatment of Hepatitis C (Foster et al.).

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Macrophage colony-stimulating factor (M-CSF) is a homodimeric cytokine that belongs to receptor tyrosine kinase subclass III of the receptor tyrosine kinase (RTK) family. M-CSF acts on a CSF-1 receptor tyrosine kinase, which initiates signaling cascades to support cell proliferation and differentiation (Hamilton). M-CSF is produced by endothelial cells, osteoblasts, and during pregnancy by the uterine epithelial cells (Ryan). M-CSF synergizes with other factors to support proliferation and differentiation of multipotent hematopoietic progenitor cells, and regulates proliferation and differentiation of the mononuclear phagocyte progenitor cells to monocytes and macrophages. It also supports survival, proliferation, and function of the differentiated macrophages and regulates differentiation of mononuclear phagocytes to osteoclasts (Pixley and Stanley). M-CSF plays an important role in the implantation of the embryo and early development (Makrigiannakis 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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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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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.).

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B cell activating factor (BAFF) is part of the tumor necrosis factor (TNF) superfamily and is expressed by monocytes, macrophages, dendritic cells, and neutrophils (Mackay and amp; Browning; Scapini et al.). It binds to 3 receptors: BAFF-R, TACI, and BCMA, all of which are expressed by B cells at various times in their development (Liu and amp; Davidson). BAFF-R signaling activates the NF-kB signaling pathway, and promotes B cell survival, Ig class switching, and antigen presentation (Bossen and amp; Schneider; Liu and amp; Davidson; Naradikian et al.). BAFF also has functions in other cell types: it promotes monocyte survival and activation, proinflammatory cytokine secretion, and differentiation into macrophages (Chang et al.), and co-stimulates anti-CD3-mediated activation of human T cells (Huard et al.; Mackay and amp; Leung).

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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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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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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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Vascular endothelial growth factor C (VEGF-C) is a member of the VEGF/platelet-derived growth factor (PDGF) family of proteins. VEGF-C is a potent angiogenic factor and promotes lymphangiogenesis, endothelial cell growth and survival, and can affect blood vessel permeability. VEGF-C is expressed in a range of tissues, but is not expressed in peripheral blood lymphocytes. VEGF-C forms a non-covalent, cell surface-associated, disulfide-linked homodimer that can bind and activate VEGF receptors 2 (VEGFR-2 [Flk1]) and 3 (VEGFR-3 [Flt4]). Interaction with VEGFR-2 results in physiological and intratumoral neoangiogenesis and vessel sprouting (Cao et al.; Tammela et al.), whereas interaction with VEGFR-3 is critical for lymphangiogenesis (Karkkainen et al.; Laakkonen et al.; Mäkinen et al.). Overexpression of VEGF-C in tumor cells has been shown to result in enhanced lymph flow and increased metastasis to regional lymph nodes (Hoshida et al.; Mandriota et al.; Padera et al.; Skobe et al.).

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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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Use visfatin to catalyse the production of nicotinamide mononucleotide from nicotinamide (Revollo et al.). Nicotinamide mononucleotide is a precursor to nicotinamide adenine dinucleotide (NAD) that is vital to energy metabolism, cell death, and other cellular processes (Ying). Visfatin also acts as an immunomodulator by activating leukocytes and inducing the production of pro-inflammatory and anti-inflammatory cytokines (Moschen et al.), and there is evidence that visfatin can regulate insulin receptor signaling and insulin secretion (Brown et al.). Belonging to the nicotinate phosphoribosyltransferase (NAPRTase) family, Visfatin is an adipokine that is produced in adipocytes, leukocytes, and hepatocytes (Chiu et al., Garten et al., Kralisch et al.). It is active as a homodimer with each identical monomer consisting of two structural domains made up of 19 β-strands and 13 α-helices (Kim et al.). For consistency and reproducibility across your applications, visfatin from STEMCELL comes lyophilised with ≥90% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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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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The principal physiological regulator of erythropoiesis, Erythropoietin (EPO) is a glycoprotein growth factor that is produced primarily in the kidney in response to hypoxia or anemia. EPO promotes erythropoiesis by binding to a homodimeric cell surface receptor that activates JAK2/STAT5, PI3K/AKT, and MAPK pathways, and stimulates the proliferation and differentiation of erythroid progenitor cells (Jelkmann. Transfus Med Hemother, 2013; Kuhrt and Wojchowski. Blood, 2015).

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

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

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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 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.).

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Persephin is a neurotrophic factor that belongs to the glial cell line-derived neurotrophic factor (GDNF) family. Persephin shares a large degree of structural similarity to GDNF, artemin, and neurturin, and has overall neuroprotective activity. Persephin signals through GRFα4 (glycosylphosphatidylinositol (GPI)-linked GDNF receptor family member) which signals through the receptor tyrosine kinase RET. Unlike GDNF and neurturin, persephin only promotes the growth and survival of central dopaminergic and motor neurons, but not peripheral neurons (Milbrandt et al.). In vitro, persephin only promotes survival of neurons that co-express GPI-linked GRFα4 and RET (Enokido et al.; Lindahl et al.). Mice lacking persephin showed increased cell death after cerebral ischemia, however administration of persephin before ischemia dramatically reduced neuronal cell death (Tomac et al.).

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CD40 ligand is a type II transmembrane glycoprotein that belongs to the tumor necrosis factor (TNF) superfamily (Quezada et al.). CD40 ligand forms a bioactive homotrimer that exists as both soluble and membrane-bound forms (Khandekar et al.). CD40 ligand is expressed on T cells, monocytes, basophils, eosinophils, platelets, dendritic cells, and endothelial cells. Its receptor, CD40, is expressed on B cells, dendritic cells, macrophages, monocytes, platelets, endothelial cells, and epithelial cells (van Kooten and Banchereau). Binding of CD40 ligand to CD40 stimulates B cell proliferation, immunoglobulin class switching, antibody secretion, and T cell-dependent humoral responses. Dysregulation of CD40 ligand contributes to immune deficiency in HIV and AIDS (Rickert et al.). CD40 ligand has also been linked to the pathology of atherosclerosis, atherothrombosis, and restenosis (Hassan et al.).

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Persephin is a neurotrophic factor that belongs to the glial cell line-derived neurotrophic factor (GDNF) family. Persephin shares a large degree of structural similarity to GDNF, artemin, and neurturin, and has overall neuroprotective activity. Persephin signals through GRFα4 (glycosylphosphatidylinositol (GPI)-linked GDNF receptor family member) which signals through the receptor tyrosine kinase RET. Unlike GDNF and neurturin, persephin only promotes the growth and survival of central dopaminergic and motor neurons, but not peripheral neurons (Milbrandt et al.). In vitro persephin only promotes survival of neurons that co-express GPI-linked GRFα4 and RET (Enokido et al.; Lindahl et al.). Mice lacking persephin showed increased cell death after cerebral ischemia, however administration of persephin before ischemia dramatically reduced neuronal cell death (Tomac et al.). This product is animal component-free.

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Neurotrophin-3 (NT-3) is a neurotrophic factor and a member of the nerve growth factor (NGF) family of proteins that includes neuron growth factor (NGF), brain-derived neurotrophic factor (BDNF), and neurotrophin-4/5. NT-3 signals a number of trophic effects through its transducing receptor tyrosine kinase TrkC. NT-3 is known to promote survival, development, and differentiation of neurons, and modulates transmitter release at several types of synapses in the peripheral and central nervous systems (Chalazonitis 1996). NT-3 has been shown to have an important role in the overall development of enteric neurons, which are crucial for gut peristalsis (Chalazonitis 2004). Studies in rats have shown the potential of NT-3 in dorsal column axonal regeneration (Bradbury et al.). NT-3 was shown to protect neurons against amyloid-β toxicity (Lesne et al.). NT-3 has applications in neuronal differentiation protocols to generate β-tubulin III+ peripheral neurons from neural crest stem cells (Menendez et al.) and oligodendrocyte precursor cells from human embryonic stem (ES) and induced pluripotent stem (iPS) cells (Douvaras 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 and bone formation and resorption (Sims and Quinn; Tanaka and Miyajima). This product is animal component-free.

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Noggin binds to and antagonizes bone morphogenetic protein (BMP) ligands of the transforming growth factor beta (TGF-β) family. Noggin supports maintenance of undifferentiated human embryonic stem cells in vitro, and can be used to prevent spontaneous differentiation in the short term (Chaturvedi et al.). Noggin is essential for development of structures derived from ectoderm embryonic somite, skeletal patterning, and neurogenesis in vivo. It also influences chondrogenesis, osteogenesis, and joint formation (Krause et al.), and promotes dopaminergic differentiation of embryonic stem cells and subsequent survival of dopamine neurons (Chiba 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).

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Macrophage inflammatory protein-1 beta (MIP-1 beta), also known as CCL4, is a member of the CC family of chemokines and is most closely related to CCL3 (MIP-1 alpha). Cellular sources of MIP-1 beta include activated leukocytes (monocytes and T and B cells), brain endothelial cells, and smooth muscle cells (Lukacs et al.; Menten et al.). MIP-1 beta, MIP-1 alpha, and RANTES have been shown to be major HIV-suppressive factors, possibly through the interactions of these chemokines with the receptor CCR5 on CD4+ T cells, which is also a major receptor for HIV entry into CD4+ T cells (Cocchi et al.; Menten et al.). MIP-1 beta attracts a variety of immune cells to sites of microbial infection. In addition to its chemotactic functions, MIP-1 beta induces the release of proinflammatory cytokines, mast cell degranulation, and NK cell activation (Schall et al.). In mice, recruitment of regulatory T cells to B cells and antigen-presenting cells by MIP-1 beta plays a central role in the initiation of T cell and humoral responses, and the depletion of regulatory T cells or MIP-1 beta results in deregulated humoral responses and production of autoantibodies (Bystry et al.).

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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.).

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Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to heterotrimeric receptors consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). High IL-2 levels in serum are associated with progression of scleroderma, rheumatoid arthritis, and gastric and non-small cell lung cancer, though no known disease can be directly attributed to the lack or excess of IL-2 (Gaffen and Liu).