Katalognummer: 209 - 101-M467
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 100 µg
101-M467
Two distinct types of receptors that bind the pleiotropic cytokines IL-1 alpha and IL-1 beta have been described. The IL-1 receptor Type I is an 80 kDa transmembrane protein that is expressed predominantly by T cells, fibroblasts, and endothelial cells. IL-1 receptor Type II is a 68 kDa transmembrane protein found on B lymphocytes, neutrophils, monocytes, large granular leukocytes and, endothelial cells. Both receptors are members of the immunoglobulin superfamily and show approximately 28% sequence similarity in their extracellular domains. The two receptor types do not heterodimerize in a receptor complex. IL-1 RII has a short cytoplasmic domain and does not transduce IL-1 signals. In addition to the membrane-bound form of IL-1 RII, a naturally-occurring soluble form of IL-1 RII has been described. It has been suggested that the Type II receptor, either as the membrane-bound or as the soluble form, serves as a decoy for IL-1 and inhibits IL-1 action by blocking the binding of IL-1 to the signaling Type I receptor complex. Recombinant IL-1 soluble receptor type II is a potent antagonist of IL-1 action.
101-M466
The Interleukin 1 receptor family comprises at least nine members. All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members also have an intracellular TIR (Toll-like receptor/IL-1 receptor) signaling domain that is also conserved in the Toll-like receptor family. A subtype of the IL-1 R family, SIGIRR (single Ig domain-containing IL-1 R-related molecule) differs from the other nine members by having only one Ig domain. IL-1 R1 is a type I transmembrane glycoprotein that functions as the ligand binding subunit in the IL-1 receptor complex. It associates with a signaling component, IL-1 R3 (IL-1 receptor accessory protein) to form a functional receptor complex for IL-1 alpha and IL-1 beta.
101-M468
The Interleukin 1 receptor family comprises at least nine members. All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members also have an intracellular TIR (Toll-like receptor/IL-1 receptor) signaling domain that is also conserved in the Toll-like receptor family. A subtype of the IL-1 R family, SIGIRR (single Ig domain-containing IL-1 R-related molecule) differs from the other nine members by having only one Ig domain. IL-1 Rrp2, also known as IL-1 R6, is a transmembrane protein belonging to the IL-1 receptor family. It is a ligand binding subunit that associates with IL-1 RAcP to form a functional receptor complex for IL-1F6, IL-1F8, and IL-1F9.
102-P155
Mouse interleukin 9 (IL-9) was originally identified as T cell-derived T cell growth factor III/P40 that could support the long term growth of certain mouse T helper clones in the absence of antigen or antigen-presenting cells. Human IL-9 was independently cloned as a novel growth factor that is mitogenic for the human megakaryoblastic leukemic cell line, M07e. Human and mouse IL-9 share 56% identity at the amino acid level. Although mouse IL-9 is active on human cells, human IL-9 is not active on mouse cells.
102-P32
Interleukin 2 (IL-2) was initially identified as a T cell growth factor that is produced by T cells following activation by mitogens or antigens. Since then, it has also been shown to stimulate the growth and differentiation of B cells, natural killer (NK) cells, lymphocyte activated killer (LAK) cells, monocytes/macrophages and oligodendrocytes. At the amino acid sequence level, there is approximately 60% - 90% similarity between species. Mature human IL-2 shows 65%, 67%, 72%, 78%, and 64% aa identity to mouse, rat, pig, cat, and cow IL-2, respectively.
102-P33
IL-3 is a hematopoietic 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 thrombopoieses, 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. IL-3 is species-specific, variably glycosylated cytokine. Recombinant human IL-3 is a 15.0 kDa globular protein containing 133 amino acid residues.

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