![]() CYTIDINE 5'-TRIPHOSPHATE DISODIUM structure
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Common Name | CYTIDINE 5'-TRIPHOSPHATE DISODIUM | ||
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CAS Number | 652154-13-7 | Molecular Weight | 527.12000 | |
Density | N/A | Boiling Point | N/A | |
Molecular Formula | C9H14N3Na2O14P3 | Melting Point | N/A | |
MSDS | USA | Flash Point | >230 °F |
Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination.
Cell. Mol. Life Sci. 71(24) , 4895-910, (2014) Membrane proteins are key elements in cell physiology and drug targeting, but getting a high-resolution structure by crystallographic means is still enormously challenging. Novel strategies are in big demand to facilitate the structure determination process t... |
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Sequence and functional analysis of the cloned Neisseria meningitidis CMP-NeuNAc synthetase.
FEMS Microbiol. Lett. 75 , 161-166, (1992) The CMP-N-acetylneuraminic acid (CMP-NeuNAc) synthetase gene of Neisseria meningitidis group B is located on a 2.3-kb EcoRI fragment within the cps gene cluster. Nucleotide sequence determination of the gene encoding the CMP-NeuNAc synthetase revealed a 515-b... |
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CTP:phosphocholine cytidylyltransferase α (CCTα) and lamins alter nuclear membrane structure without affecting phosphatidylcholine synthesis.
Biochim. Biophys. Acta 1811 , 377-385, (2011) CTP:phosphocholine cytidylyltransferase α (CCTα) is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine (PC) synthesis. Lipid activation of CCTα results in its translocation to the nuclear envelope and exp... |
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The Kap60-Kap95 karyopherin complex directly regulates phosphatidylcholine synthesis.
J. Biol. Chem. 284 , 7376-7384, (2009) Phosphatidylcholine is the major phospholipid in eukaryotic cells. There are two main pathways for the synthesis of phosphatidylcholine: the CDP-choline pathway present in all eukaryotes and the phosphatidylethanolamine methylation pathway present in mammalia... |
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Purification of CMP-N-acetylneuraminic acid synthetase from bovine anterior pituitary glands.
Glycobiology 9 , 481-487, (1999) CMP-beta-N-acetylneuraminic acid (CMP-neuNAc) is the substrate for the sialylation of glycoconjugates by sialyltransferases in microbes and higher eukaryotes. CMP-neuNAc synthetase catalyzes the formation of this substrate, CMP-neuNAc, from CTP and neuNAc. In... |
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