303 Results for: "Shenandoah Biotechnology"

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Interleukin 35 (IL-35) is a member of the IL-12 cytokine family and is produced by regulatory T cells (Tregs). IL-35 is a heterodimeric cytokine that is comprised of the interleukin 12 subunit P35 (IL-12a) and the interleukin 27 subunit beta (IL-27b) chains. IL-35 binds the IL-12Rbeta2/gp130 hetero- and homodimers to activate STAT1 and STAT4 signaling. IL-35 functions as a suppressor of immune cell inflammatory responses.

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Epidermal growth factor (EGF) is a growth factor that stimulates the proliferation, differentiation, and survival of epithelial and epidermal cells. EGF contains three intramolecular disulfide bonds and binds in high affinity to the epidermal growth factor receptor (EGFR).

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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. Animal-free.

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Interleukin 36 gamma (IL-36γ) is a member of the interleukin 1 (IL-1) cytokine family and protects against pathogens in the skin, lung, and stomach epithelial barriers. IL-36G binds the interleukin-1 receptor accessory protein (IL-1RAcP) and the orphan IL-1R-related protein 2 (IL-1Rrp2) receptors to activate NF-kB and MAP kinase signaling pathways, resulting in the induced production of inflammatory cytokines and chemokines. Animal-free.

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Interleukin 17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites.  Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis.  Human, mouse, and rat IL-17A show activity on mouse cells. 

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Mouse IL-6 recombinant protein, Purity: >/=95%, Source: E.coli, MW: Monomer, 21.9 kDa (188 aa), Endotoxin: /=2.0 x 10power 7 units/mg), Synonym: IFN-B2, B-cell Differentiation Factor, BSF-2, HSF, MGI-2, Size: 100UG

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Interleukin 17F (IL-17F), a member of the IL-17 cytokine family, is secreted by activated CD4+ T cells and monocytes. IL-17F binds the IL-17 receptor related molecule, IL17RC, to promote the production of the interleukin 6 (IL-6), interleukin 8 (IL-8), and granulocyte macrophage colony-stimulating factor (GM-CSF) cytokines. IL-17F also functions to regulate matrix turnover rates, inhibit endothelial cell angiogenesis, and induce the endoethelial cell expression of interleukin 2 (IL-2), monocyte chemoattractant protein-1 (MCP-1), and transforming growth factor beta 1 (TGF-b1).

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Interleukin 22 (IL-22), also called IL-TIF, is an IL-10 family member that is produced by activated dendritic cells and T lymphocytes. It signals via a heteroduplex receptor consisting of IL-22R and IL-10Rbeta chains. It is a potent mediator of cellular inflammatory responses and wound healing.

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Glial cell-derived neurotrophic factor (GDNF) is a neurotrophic factor that signals through a multicomponent receptor system to activate receptor tyrosine kinase RET signaling. GDNF promotes dopamine uptake, prevents motor neuron apoptosis, and supports the survival and differentiation of neurons.

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Epidermal growth factor (EGF) is a growth factor that stimulates the proliferation, differentiation, and survival of epithelial and epidermal cells. EGF contains three intramolecular disulfide bonds and binds in high affinity to the epidermal growth factor receptor (EGFR).

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Platelet-derived growth factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by interleukin 1 (IL-1), interleukin 6 (IL-6), tumor necrosis factor alpha (TNFα), transforming growth factor beta (TGF-β), and epidermal growth factor (EGF) signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the alpha-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

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Platelet-derived growth factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-a, TGF-b and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the alpha-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

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Mouse leukemia inhibitory factor (LIF) is a member of the interleukin 6 (IL-6) family that is made by a variety of adult and embryonic tissues. LIF signals through the glycoprotein 130 (gp130)/LIF receptor (LIFR) heterodimer to activate STAT3 and MAPK signaling. LIF functions during hematopoietic differentiation, neuronal cell differentiation, kidney development, and inflammatory processes. The application of mouse LIF to long-term culture systems promotes mouse embryonic stem (ES) cell self-renewal and pluripotency, similar to the functional activity of bFGF (FGF2) in human ES cell culture systems.

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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. Mouse VEGF-A has several alternatively spliced isoforms, with one being VEGF-120. VEGF-120 is an angiogenic factor that is expressed throughout endochondral bone development and is important during skeletogenesis.

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Stromal cell-derived factor-1 beta (SDF-1β), also called CXCL12b, is one of two SDF-1 splice variants made by a wide variety of cells upon stimulation by inflammatory cytokines such as tumor necrosis factors (TNF), interleukin 1 (IL-1), and lipopolysaccharide (LPS). SDF-1β signals through the G protein-coupled receptor CXCR4 to recruit activated leukocytes.

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Resistin-like molecule-beta (RELM-β) is a member of the RELM family of secreted proteins containing conserved C-terminus cysteines. The RELM family consists of Resistin (FIZZ3), RELM-α (FIZZ1), RELM-β (FIZZ2), and RELM-γ (FIZZ4). Resistin and RELM-β are the only RELM family members found in humans, whereas all four RELM family members are present in rodents. RELM-β functions to increase fibroblast proliferation and differentiation, resulting in airway remodelling and increased inflammation.

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Basic fibroblast growth factor (bFGF), also known as FGF2, is expressed by endothelial cells and is a mediator of angiogenesis. bFGF also has cardioprotective functions during heart injury. bFGF binds heparin in order to signal through fibroblast growth factor (FGF) receptor tyrosine kinases.

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Receptor activator of nuclear factor kappa-B Ligand (RANKL) is a cell-bound marker related to the tumor necrosis factor (TNF) family of proteins. RANKL plays a critical role in bone metabolism and osteoclast differentiation. T cell expression of RANKL promotes dendritic cell maturation.

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Oncostatin M (OSM) is a cytokine that is produced by macrophages, dendritic cells, and T lymphocytes during inflammatory events. The Type-I and Type-II OSM receptors are located on the cell surface of endothelial and tumor cells, contain the glycoprotein 130 (gp130) subunit, and activate the JAK/STAT signaling pathway. OSM functions to inhibit tumor cell proliferation, induce liver stem cell maturation, regulate cytokine production during hematopoiesis and inflammation, stimulate bone formation, and promote nervous system development.

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Platelet-derived growth factor (PDGF) is an important regulator of cell growth, proliferation, and angiogenesis. PDGF synthesis is induced by IL-1, IL-6, TNF-a, TGF-b and EGF signaling. PDGF functions as a mitogenic growth hormone on cells of mesenchymal lineage, such as smooth muscle and glial cells. PDGF is also stored in the alpha-granules of platelets and is released upon adherence to traumatized tissues. PDGF is a dimeric glycoprotein formed by two A chains (AA), two B chains (BB), or as a heterodimer with an A and a B chain (AB). The PDGF dimer binds the cell surface receptor tyrosine kinases PDGFR-a and PDGFR-b.

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Insulin-like growth factor I (IGF-I) is a growth factor that is produced by the liver. IGF-1 production is stimulated by growth hormone (GH). IGF-I binds the insulin-like growth factor 1 receptor (IGF1R) and the insulin receptor to stimulate systemic body growth. IGF-I is one of the most potent activators of the AKT signaling pathway, which stimulates cell proliferation and inhibits programmed cell death. Mature human IGF-I is 100% homologous to bovine and porcine IGF-1 proteins.

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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. Adult GH deficiency presents with reduced lean body mass, increased adiposity, reduced muscle strength, and ultimately premature mortality. GH replacement therapy is used to treat many growth disorders, including Turner syndrome, chronic renal failure, and Prader–Willi syndrome.

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The globular subunit of adipocyte complement-related protein of 30 kDa (gACRP30) is a naturally occurring cleavage product of adiponectin, a protein made exclusively by adipocytes. gACRP30 is an abundant serum protein and plays an important role in hyperglycemia, insulin resistance, and fatty acid oxidation. gACRP30 signals through adiponectin receptor 1 (AdipoR1) and adiponectin receptor 2 (AdipoR2).

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Galectin-3 belongs to the lectin family of carbohydrate binding proteins. Galectin-3 is expressed by a wide range of cell types including activated T cells, tumor cells, macrophages, osteoclasts, fibroblasts, and epithelial cells. Galectin-3 has specific binding affinity for beta-galactoside sugar moieties and has functional roles during development, innate immunity, cell apoptosis, and tumor metastasis. Galectin-3 is associated with cancer, heart failure, stroke, and inflammation. The amino acid sequences of human and mouse Galectin-3 proteins share 80% homology.

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Persephin (PSP) is a neurotrophic factor of the glial cell line-derived neurotrophic factor (GDNF) family. PSP promotes survival and growth of dopaminergic and motor neurons, but not peripheral neurons. PSP is a ligand for the RET receptor tyrosine kinase.

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Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a member of the tumor necrosis factor (TNF) family of cytokines. TRAIL is widely produced by a variety of cell types including tumor cells, smooth muscle of the lung and spleen, cerebellar glial cells, and thyroid follicular cells. TRAIL is a cytotoxic protein that induces apoptosis in tumor cells through the activation of the death receptors DR4 and DR5. TRAIL also binds the neutralizing decoy receptors, DcR1 and DcR2. Human TRAIL is active on mouse cells.

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Macrophage inflammatory protein-3 beta (MIP-3-beta), also called CCL19, is a chemokine that is expressed in the thymus, lymph nodes, and activated bone marrow stromal cells. MIP-3-beta signals through the G protein-coupled receptor CCR7 to regulate normal lymphocyte recirculation. MIP-3-beta also functions during T cell trafficking to the thymus, and in T cell and B cell homing to the lymph nodes and secondary lymphoid organs. Human MIP-3-beta shows activity on mouse cells.

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Tumor necrosis factor alpha (TNFa) is an inflammatory cytokine secreted by macrophages, monocytes, neutrophils, T cells, and NK-cells following stimulation by bacterial lipopolysaccharide (LPS). TNFa signal activation occurs through two receptors, TNFR1 and TNFR2. TNFR1 is expressed on most cell types, unlike TNFR2, which is expressed mainly on immune cells. TNFa functions to stimulate phagocytosis in macrophages, chemoattract neutrophils, increase insulin resistance, and induce fever.

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Prolactin (PRL) is a hormone that is produced and secreted by the pituitary gland. PRL acts in an endocrine, paracrine, and autocrine manner. The prolactin receptor (PRLR) is expressed on many cell types, including cells of the reproductive organs, central nervous system, and breast cancer. PRL signal transduction occurs via JAK kinase signaling pathways. The primary function of PRL is to regulate lactation, but PRL also plays functional roles in the immune system and during cell growth, apoptosis, and differentiation.

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Pleiotrophin (PTN) is a heparin-binding growth factor that has mitogenic effects on fibroblast, epithelial, and endothelial cells. PTN is made by many tissues, but is predominantly secreted by nervous tissue during development. PTN induces neurite outgrowth and is involved in tumor growth and metastasis. PTN binds with low affinity to the cell surface receptor nucleolin to inhibit HIV-1 infection. PNT also binds the receptor protein tyrosine phosphatase type Z (PTPRZ), syndecan-3, and anaplastic lymphoma kinase (ALK) receptors.