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胞嘧啶核苷5`-三磷酸二钠盐水合物

胞嘧啶核苷5`-三磷酸二钠盐水合物结构式
胞嘧啶核苷5`-三磷酸二钠盐水合物结构式
品牌特惠专场
常用名 胞嘧啶核苷5`-三磷酸二钠盐水合物 英文名 CYTIDINE 5'-TRIPHOSPHATE DISODIUM
CAS号 652154-13-7 分子量 527.12000
密度 N/A 沸点 N/A
分子式 C9H14N3Na2O14P3 熔点 N/A
MSDS 美版 闪点 >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...

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...

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...

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...

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...