Results for Cytokines & Chemokines ( 1799 )
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Galectin-9 is a cytoplasmic protein that contains two galectin domains. Galectin-9 is an S-type lectin that is over-expressed in Hodgkin's disease tissue. Galectin-9 binds galactosides and has high affinity for the Forssman pentasaccharide. Galectin-9 plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. Galectin-9 is a ligand for HAVCR2/TIM3 and induces T-helper type 1 lymphocyte (Th1) death. In addition, Galectin-9 suppresses tumor cell metastasis by interfering with the associations CD44, VCAM-1, Integrin α4β1.
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Galectin-9 is a cytoplasmic protein that contains two galectin domains. Galectin-9 is an S-type lectin that is over-expressed in Hodgkin's disease tissue. Galectin-9 binds galactosides and has high affinity for the Forssman pentasaccharide. Galectin-9 plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. Galectin-9 is a ligand for HAVCR2/TIM3 and induces T-helper type 1 lymphocyte (Th1) death. In addition, Galectin-9 suppresses tumor cell metastasis by interfering with the associations CD44, VCAM-1, Integrin α4β1.
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Cell surface glycoprotein CD200 Receptor 1 (CD200R1) is the receptor for the CD200 (OX-2) membrane glycoprotein. CD200R1 contains one C2- type Ig-like domain and one V-type Ig-like domain within its extracellular domain and a PTB-signaling motif in cytoplasmic domain. CD200R1 and CD200 associate via their respective N-terminal Ig-like domains. CD200R1 is restricted primarily to mast cells, basophils, macrophages, and dendritic cells. It propagates inhibitory signals despite its lacking a cytoplasmic ITIM (immunoreceptor tyrosinebased inhibitory motif). The receptor-substrate interaction may function as a myeloid downregulatory signal.
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Insulin-like growth factor 1 (IGF-1), also called Somatomedin, is a hormone similar in molecular structure to insulin but has a much higher growth-promoting activity. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. It is able to stimulate glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. It may also play a role in synapse maturation.
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Insulin-like growth factor 1 (IGF-1), also called Somatomedin, is a hormone similar in molecular structure to insulin but has a much higher growth-promoting activity. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. It is able to stimulate glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. It may also play a role in synapse maturation.
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Insulin-like growth factor 1 (IGF-1), also called Somatomedin, is a hormone similar in molecular structure to insulin but has a much higher growth-promoting activity. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. It is able to stimulate glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. It may also play a role in synapse maturation.
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Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, PDGF-AB. It is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).
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Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, PDGF-AB. It is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).