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Growth hormone (GH) is an important mitogenic growth factor that is synthesized, stored, and secreted by somatotropic cells of the anterior pituitary gland. GH stimulates growth, cell reproduction, and cell regeneration. In children, GH deficiencies can cause short stature, growth failure, and delayed sexual maturity.

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IL-15 is a widely expressed proinflammatory cytokine that is structurally and functionally related to IL-2. Signals through JAK kinases to activate STAT3, STAT5, and STAT6 transcription factors. Regulates the activation of T cells, neutrophils, and macrophages, and is a stimulatory cytokine promoting dendritic cell function.

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Fibroblast growth factor 5 (FGF-5) is a secreted heparin-binding growth factor that binds to FGF receptors 1 and 2 (FGFR1 and FGFR2). FGF-5 is expressed in the mesenchyme, skeletal muscles, central nervous system, and hair follicles to promote cell differentiation and proliferation. FGF-5 functions as a regulatory factor during hair elongation and skeletal muscle development.

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Interleukin 16 (IL-16) is produced by CD4+ and CD8+ T cells and functions as a chemoattractant for lymphocytes, monocytes, eosinophils, dendritic cells, and langerhans cells.  Additionally, IL-16 upregulates the expression of the interleukin 2 receptor (CD25), modulates T lymphocyte growth, and suppresses the replication of the human immunodeficiency virus (HIV) and simian immunodeficiency viruses (SIV).

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Interleukin 11 (IL-11) is a member of the gp130 family of cytokines. IL-11 functions to promote hematopoietic stem cell proliferation and megakaryocyte differentiation. In non-hematopoietic cell populations, IL-11 stimulates acute-phase proteins, modulates the development of immunoglobulin-producing B cells, and regulates bone turnover. IL-11 binds the IL-11Rα receptor to activate JAK downstream signaling.

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Interleukin 32 alpha (IL-32 α) is one of six known splice variants of the IL-32 gene. IL-32 α induces the macrophage production of inflammatory cytokines, such as interleukin 8 (IL-8), tumor necrosis factor-alpha (TNF-α), and macrophage inflammatory protein 2 (MIP-2). IL-32 α expression is increased after the activation of T cells, natural killer (NK) cells, and interferon gamma-treated epithelial cells.

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Fms-related tyrosine kinase 3 ligand (FLT-3 ligand) is a growth factor that regulates hematopoietic cell proliferation. FLT-3 ligand signaling is transmitted through the fms-related tyrosine kinase 3 (FLT-3) receptor. FLT-3 ligand promotes the long-term expansion and differentiation of pro-B cells in the presence of interleukin 7 (IL-7) or in combination of IL-7 and interleukin 3 (IL-3).

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Interleukin 1 alpha (IL-1α) is expressed by epithelial cells, activated macrophages, neutrophils, and endothelial cells to regulate immune responses. IL-1α signals through the IL-1 receptor, type 1 (IL-1R1) to activate the myeloid differentiation primary response 88 (MYD88) signaling pathway, which contains the cytoplasmic Toll/IL-1 receptor (TIR) domain adapter.

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Connective tissue growth factor (CTGF) is a mitogen that is secreted by vascular endothelial cells in response to basic fibroblast growth factor (bFGF) or vascular endothelial growth factor (VEGF). CTGF promotes cell growth, migration, adhesion, and survival of endothelial cells. CTGF is also important during osteogenesis, chondrogenesis, and skeletogenesis. CTGF has an insulin-like growth factor binding protein (IGFBP) domain, a thrombospondin type 1 repeat (TSR) domain, and a C-terminal cysteine knot motif.

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Acidic fibroblast growth factor (FGF-acidic), also known as FGF-1, is a potent inducer of DNA synthesis, cell proliferation, and has chemotactic activities. FGF-acidic regulates cardiogenesis through protein kinase C signaling. FGF-acidic also functions as an insulin sensitizer and mediates adipose tissue remodeling. High serum levels of FGF-acidic are associated with type 2 diabetes mellitus (T2DM), suggesting a pathogenic role of FGF-acidic during T2DM.

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Interleukin 11 (IL-11) is a member of the gp130 family of cytokines. IL-11 functions to promote hematopoietic stem cell proliferation and megakaryocyte differentiation. In non-hematopoietic cell populations, IL-11 stimulates acute-phase proteins, modulates the development of immunoglobulin-producing B cells, and regulates bone turnover. IL-11 binds the IL-11Rα receptor to activate JAK downstream signaling. Human IL-11 shows activity on murine cells.

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Vascular endothelial growth factor-A (VEGF-A) is produced by a wide variety of cell types, including tumor and vascular cells. VEGF-A is a mediator of vascular growth, vascular permeability, and plays a role in stimulating vasodilation via nitric oxide-dependent pathways. VEGF-A has several alternatively spliced isoforms, with VEGF-165 being the most abundant. The VEGF-165 isoform is a secreted protein that acts on receptors VEGFR-1 and VEGFR-2 to modulate endothelial cell proliferation and angiogenesis.

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GM-CSF is a hematopoietic growth factor with the ability to form colonies of granulocytes and macrophages. Enhances the number of circulating white blood cells and function of neutrophils and monocytes. Regulates multiple functions via transcription factors in the differentiated cells, including cell survival, proliferation, and maturation. Generates in vitro murine and human DC populations from bone marrow precursors and blood monocytes, respectively.

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Cytokines for polarizing human T cells into Th9 cells. Th9 cells are a unique subset of T helper cells that produce IL-9. An important function of IL-9 producing T cells is fighting inflammation and helminth infections. Th9 cells can be generated from naive CD4+ T cells in culture by culturing them in the presence of IL-4 and TGF-β 1. It also appears that IFNγ and IL-27 can inhibit the generation of Th9 cells.

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Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) is an angiogenic growth factor that is expressed in the ovaries, testis, adrenal, and placental tissues. EG-VEGF has mitogenic, chemoattractive, and antiapoptotic functional roles. EG-VEGF signaling is mediated through binding the G protein-coupled receptors prokineticin receptor 1 (PKR1) and prokineticin receptor 2 (PKR2). Polycystic ovaries display strong EG-VEGF expression that is associated with increased angiogenesis and cyst formation, which could lead to the formation of polycystic ovary syndrome and infertility.

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Resistin-like molecule-gamma (RELM-γ) is a member of the RELM family of secreted proteins containing C-terminal cysteines. The RELM family consists of Resistin (FIZZ3), RELM-α (FIZZ1), RELM-β (FIZZ2), and RELM-γ (FIZZ4). RELM-γ is secreted by peripheral blood granulocytes, bone marrow, spleen, intestine, and lung. RELM-γ functions to promote and regulate promyelocytic differentiation, in addition to regulating nutrient-associated insulin sensitivity in the intestinal tract. Rodents secrete all four RELM family members, whereas Resistin and RELM-β are the only RELM family members found in humans.

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Interleukin 12 (IL-12) is an inducer of cell-mediated immunity and is produced by dendritic cells, macrophages, and B cells after antigen stimulation. IL-12 functions to promote naïve T cell differentiation into the type 1 T helper cell (Th1) lineage. IL-12 also stimulates the production of interferon gamma (IFN-γ) and tumor necrosis factor alpha (TNF-α) from T cells and natural killer cells. Mouse IL-12 is active on human and mouse cells.

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Epstein-Barr virus induced gene-3 (EBI3) is a secreted glycoprotein belonging to the hematopoietin receptor family related to the p40 subunit of interleukin 12 (IL-12). EBI3 expression is induced in B-lymphocytes in response to Epstein-Barr virus infection. EBI3 forms heterodimers with p28 to form interleukin 27 (IL-27), and with p35 to form interleukin 35 (IL-35). Both IL-27 and IL-35 have anti-inflammatory and regulatory activity.     

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Interleukin 1 alpha (IL-1α) is expressed by epithelial cells, activated macrophages, neutrophils, and endothelial cells to regulate immune responses. IL-1α signals through the IL-1 receptor, type 1 (IL-1R1) to activate the myeloid differentiation primary response 88 (MYD88) signaling pathway, which contains the cytoplasmic toll/IL-1 receptor (TIR) domain adapter. IL-1α and the independently regulated IL-1β protein have overlapping proinflammatory activities to induce adhesion molecule expression on epithelial cells, control fever induction, initiate rheumatoid arthritis, and promote septic shock.

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Cytokines for expansion and cell culture of human hematopoietic stem cells to progenitor cells. Hematopoietic stem cells are self renewing pluripotent cells often characterized by the expression of CD34. Studies have shown that decreased expression of CD34 tends to correlate with the decreased self renewal properties and pluripotent potential. Culturing CD34+ cells in a cytokine mixture of SCF, FLT-3 Ligand, IL-6 and IL-3 for short time periods allows rapid expansion of immature and more mature hematopoietic progenitor cells in cord blood or bone marrow preparations.

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Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family and promotes endothelial cell growth and angiogenesis. PlGF is secreted as a homodimer and may also form a heterodimer with VEGF. PlGF is detected in the placenta, heart, lungs, thyroid, and adipose tissues. Circulating PlGF levels are correlated with colorectal and renal cancers, as well as atherosclerosis and ischemic heart disease. There are four alternatively spliced PlGF isoforms (PlGF-1, PlGF-2, PlGF-3, and PlGF-4), each with unique secretion patterns and heparin-binding affinities. PlGF-3 lacks a heparin-binding domain and signals through the VEGFR-1 receptor.

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Heparin-binding EGF-like growth factor (HB-EGF) is a member of the epidermal growth factor (EGF) family and is expressed by monocytes and macrophages. HB-EGF is the predominant growth factor involved in epithelialization during wound healing. HB-EGF signals through the receptor tyrosine kinase ErbB2 to maintain adult heart homeostasis, and promotes cardiac valve development through binding in high affinity to the epidermal growth factor receptor (EGFR). HB-EGF binds the the ErbB4 receptor tyrosine kinase to mediate implantation of the human blastocyst. HB-EGF also functions as a potent mitogen for fibroblasts and smooth muscle cells.

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Interleukin 15 (IL-15) is a widely expressed proinflammatory cytokine that is structurally and functionally related to interleukin 2 (IL-2). IL-15 signals through JAK kinases to activate STAT3, STAT5, and STAT6 transcription factors. IL-15 regulates the activation of T cells, neutrophils, and macrophages, and is a stimulatory cytokine promoting dendritic cell function. IL-15 expression is dysregulated in chronic inflammatory disorders, including rheumatoid arthritis, psoriasis, and pulmonary inflammatory diseases. Therefore, IL-15 may serve as an effective therapeutic target, due to the beneficial outcomes of IL-15 neutralization in models of psoriasis and diabetes. Human IL-15 shows activity on mouse cells.

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IL-3 is a species-specific cytokine and pleiotropic growth factor that promotes the survival, differentiation, and proliferation of committed progenitor cells of the megakaryocyte, granulocyte-macrophage, erythroid, eosinophil, basophil, and mast cell lineages. Produced by T cells, mast cells, and eosinophils, IL-3 enhances thrombopoiesis, phagocytosis, and antibody-mediated cellular cytotoxicity. Its ability to activate monocytes suggests that IL-3 may have additional immunoregulatory roles. Many of the IL-3 activities depend upon co-stimulation with other cytokines. The biological activity of CTGrade GMP interleukins and growth factors is standardized, where applicable, to WHO International standards, providing cell and gene therapy developers consistent, lot-to-lot biological activity and performance.

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Cytokines for the differentation of human monycyte-derived dendritic cells. Dendritic cells are an important type of immune cell that function to activate T and B cells via their role as an antigen presenting cell. Monocytes isolated from peripheral blood can be differentiated to immature dendritic cells (iDCs) through culturing in the presence of interleukin-4 (IL-4) and granulocyte-macrophage colony stimulating factor (GM-CSF). The characteristics of monocyte-derived iDCs are detectable after culture with IL-4/GM-CSF and include: the down regulation of CD14 surface expression, an increase in dextran uptake and an increased response to MIP-1α. Subsequent culturing with pro-inflammatory cytokines (such as TNF-α, IL-1β, and IL-6) can further differentiate the iDCs into mature dendritic cells (mDCs) that have full T cell stimulating capacity. This bundle includes 1X 100 μg of Recombinant Human IL-4 and 1X 100 μg of Recombinant Human GM-CSF.

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Transforming growth factors (TGFs) are multifunctional peptides that regulate growth and differentiation in most cell types. The TGF-β family of proteins signal through serine/threonine kinase receptors. TGF-β isoforms (TGF-β1, -β2, and –β3) have overlapping, yet distinct biological actions in developing and adult tissues. TGF-β3 is an important factor in regulating cell adhesion and accelerating wound repair. TGF-β3 also functions during osteoblast proliferation, chemotaxis, and collagen synthesis.

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Growth regulated protein gamma (GRO-ɣ), also called CXCL3, acts through the chemokine receptor CXCR2 to promote monocyte migration and adhesion. GRO-ɣ also induces the migration of cerebellar granule neuron precursor cells.

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Bone morphogenetic protein 2 (BMP-2) is a member of the bone morphogenetic protein (BMP) family and functions as a potent inducer of bone and cartilage development. BMP proteins are synthesized as large precursor molecules which are cleaved by proteolytic enzymes. Active BMP-2 consists of forming a homodimer or a heterodimer with a related BMP, such as BMP-7.

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Neurotrophin-4 (NT-4) is an important member of the nerve growth factor (NGF) family of proteins. Neurotrophins undergo paracrine and autocrine signaling to control neuronal survival, neuronal differentiation, and dendrite outgrowth. NT-4 is expressed ubiquitously and signals through the TrkB receptor tyrosine kinase.

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Bone morphogenetic protein 2 (BMP-2) is a member of the bone morphogenetic protein (BMP) family and functions as a potent inducer of bone and cartilage development. BMP proteins are synthesized as large precursor molecules which are cleaved by proteolytic enzymes. Active BMP-2 consists of forming a homodimer or a heterodimer with a related BMP, such as BMP-7.