"Bioss"

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Cytidine is a nucleoside formed by a cytosine attached to a ribose ring via a beta-N1-glycosidic bond. DNA is methylated on cytidines by DNA methylases (DNMTs)to generate 5-methylcytidine (5-mC), a potent epigenetics marker and regulator of gene expression. The reverse reaction (cytidine demethylation) starts with its oxidation to hydroxymethyl- (5-hmC), formyl- (5-fC), and carboxy- (5-caC) cytidine. Several enzymes, including the Tet family of proteins have been implicated in cytidine demethylation.

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Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle.

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Facilitative glucose transporter. Probably a neuronal glucose transporter.

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Claudin 1-8 proteins are a family of transmembrane proteins associated with tight junctions. Tight junctions are specialized regions of cell to cell contact made up of network of strands that act as a molecular gasket for preventing the leakage of ions, water etc. between cells. They are abundant in luminal epithelial sheets where they maintain epithelial cell polarity. Different tissues exhibit different Claudin composition.

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General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity (By similarity).

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Chicken Interleukin 4 (IL4) ELISA Kit

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SMYD3 is a gene that is over-expressed in the majority of colorectal carcinomas and hepatocellular carcinomas. SMYD3 forms a complex with RNA polymerase II through an interaction with the RNA helicase HELZ and transactivates a set of genes that included oncogenes, homeobox genes and genes associated with cell-cycle regulation. SMYD3 binds to a motif, 5'-CCCTCC-3', present in the promoter region of downstream genes such as Nkx2.8. The SET domain of SMYD3 shows histone H3-lysine 4 (H3-K4)-specific methyltransferase activity, which is enhanced in the presence of the heat-shock protein HSP90A.

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Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases, such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD50 (ankyrin repeat domain 50) is a 1,429 amino acid phosphoprotein that contains nineteen ANK repeats. Conserved in chimpanzee, dog, cow, mouse, rat, chicken, zebrafish, fruit fly and mosquito, ANKRD50 is encoded by a gene that maps to human chromosome 4q28.1. Chromosome 4 represents approximately 6% of the human genome and contains nearly 900 genes. Notably, the Huntingtin gene, which encodes an expanded glutamine tract in cases of Huntington's disease, is located on chromosome 4. FGFR-3 is also encoded by a gene that maps to human chromosome 4 and has been associated with thanatophoric dwarfism, achondroplasia, Muenke syndrome and bladder cancer. Chromosome 4 is also linked to Ellis-van Creveld syndrome, methylmalonic acidemia and polycystic kidney disease.

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ZNRF4 contains 1 PA (protease associated) domain and 1 RING-type zinc finger.

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Microfibrillar-associated protein 1; MFAP1_HUMAN.

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The protein encoded by this gene catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The encoded protein is a type II integral membrane protein found in the Golgi body. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].

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Anti-ADAM17 Rabbit Polyclonal Antibody

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p38 is a 38 kDa Stress Activated Protein Kinase/Map Kinase (SAPK/MAPK) that is fully activated by dual phosphorylation on threonine 180 and tyrosine 182, within the activation loop. p38 MAPK plays a critical role in the initiation of G2 delay after ultraviolet radiation; gene knock out studies have also revealed a critical role for p38 in cardiac remodeling. Downstream targets of p38 include the transcription factors ELK1 and ATF2 and the kinases MAPKAPK2 and MAPKAPK5. p38 MAPK plays a role in the production of IL6 and is thought to stabilize erythropoietin production during hypoxic stress. It is activated by environmental stress, many proinflammatory cytokines and lipopolysaccharide. Dual phosphorylation by MAP2K3 and MAP2K6 is required for activation of p38 MAPK. It interacts with MAX, Cdc25B, Cdc25C and binds to the kinase interaction domain in the protein tyrosine phosphatase PTPRR; this interaction retains p38 MAPK in the cytoplasm.

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Luciferase from the firefly has become one of the more widely used reporter proteins for the study of gene expression. Luciferase catalyzes a bioluminescent reaction which requires the substrate luciferin as well as Mg2+ and ATP. Mixing these reagents with the cell extract containing luciferase, results in a flash of light that decays rapidly. This light can be detected by a luminometer. The total light emission is proportional to the luciferase activity of the sample.

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Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

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Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.