|Related Categories||2.7.x.x Phosphorus containing groups, 2.x.x.x Transferases, Application Index, Biochemicals and Reagents, Carbohydrate hydrolysis & PTM analysis,|
|recombinant||expressed in E. coli BL21|
|shipped in||dry ice|
Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 8.5) containing Neu-5-Ac (1 mM) and CTP (1 mM) at 37 °C for 30 min and analyzed using capillary electrophoresis with a UV detector (200 nm).
One unit will catalyze the formation of 1 μmol CMP-Neu-5-Ac from Neu-5-Ac and CTP per minute at 37 °C at pH 8.0.
Supplied as a lyophilized powder containing Tris-HCl and NaCl.
The enzyme has been utilized to synthesize CMP-sialic acid and its derivatives.1
Customers Also Viewed
recombinant, expressed in E. coli BL21, ≥2 units/mg protein
recombinant, expressed in E. coli BL21, ≥5 units/mg protein
From our library of Related Content, Sigma-Aldrich presents Enzyme Explorer: the most comprehensive source of enzymes, substrates, activators, & inhibitors.
Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
1. Chemoenzymatic synthesis of CMPsialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP-sialic acid synthetases. Yu H, et al. Bioorg. Med. Chem. 12, 6427-6435, (2004)
Purification and characterization of the recombinant CMP-sialic acid synthetase from Neisseria meningitides. Gilbert, M., et al Biotechnol. Lett. 19, 417-420, (1997)
Identification of the nuclear export signals that regulate the intracellular localization of the mouse CMP-sialic acid synthetase. Fujita A, Sato C, and Kitajima K Biochem. Biophys. Res. Commun. 355(1), 174-80, (2007)
Addition of neuA, the gene encoding N-acylneuraminate cytidylyl transferase, increases the discriminatory ability of the consensus sequence-based scheme for typing Legionella pneumophila serogroup 1 strains. Ratzow S, Gaia V, Helbig JH, et al. J. Clin. Microbiol. 45(6), 1965-8, (2007)
Direct detection of ligand binding to Sepharose-immobilised protein using saturation transfer double difference (STDD) NMR spectroscopy. Haselhorst T, Münster-Kühnel AK, Oschlies M, et al. Biochem. Biophys. Res. Commun. 359(4), 866-70, (2007)
The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme. Tiralongo J, Fujita A, Sato C, et al. Glycobiology 17(9), 945-54, (2007)
A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme. Oschlies M, Dickmanns A, Haselhorst T, et al. J. Mol. Biol. 393(1), 83-97, (2009)
Identification and characterization of important residues in the catalytic mechanism of CMP-Neu5Ac synthetase from Neisseria meningitidis. Horsfall LE, Nelson A, Berry A. FEBS J. 277, 2779-2790, (2010)
A CMP-N-acetylneuraminic acid synthetase purified from a marine bacterium, Photobacterium leiognathi JT-SHIZ-145. Kajiwara H, Mine T, Miyazaki T, et al. Biosci. Biotechnol. Biochem. 75(1), 47-53, (2011)
Pasteurella multocida CMP-sialic acid synthetase and mutants of Neisseria meningitidis CMP-sialic acid synthetase with improved substrate promiscuity. Li Y, Yu H, Cao H, et al. Appl. Microbiol. Biotechnol. 93(6), 2411-23, (2012)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Need larger quantities for your development, manufacturing or research applications?