2.7.7.43	-	706038	
2.7.7.43	a series of deletions from the 3'-end of the CMP-NeuAc synthetase coding region is constructed and expressed in Escherichia coli	662202	
2.7.7.43	cloned in Escherichia coli as a His6-tagged fusion protein	672738	
2.7.7.43	cloned in Escherichia coli XL-10	671567	
2.7.7.43	cloning is achieved by complementation of the Chineses hamster ovary lec32 mutation that causes a deficiency in CMP-N-acetylneuraminate synthetase activity, it also causes polysialic acid to be expressed in the capsule of the CMP-Neu5Ac synthetase negative Escherichia coli mutant EV5	645273	
2.7.7.43	DmCSAS is cloned into the baculovirus vector pBlueBac4.5 (pBlueBac-DmCSAS4) which is used to transfect LEC29.Lec32 cells	674570	
2.7.7.43	DNA and amino acid sequence determination and analysis, when expressed in Drosophila S2 cells, DmCSS is mainly secreted into the culture medium, although partially detected in Golgi. Transient functional recombinant expression of myc-tagged wild-type and mutant enzymes in LEC29. Lec32 cells which lack a functional CSS, recombinant expression of His-tagged DmCSS in Escherichia coli	761215	
2.7.7.43	DNA and amino acid sequence determination and analysis, when expressed in mammalian and insect cells, recombinant AaCSS shows in vivo and in vitro CSS activities. In contrast, when expressed in bacteria, it lacks CSS activity because the N-terminal hydrophobic region appears to induce protein aggregation, when expressed as C-terminally V5-tagged enzyme in Drosophila S2 cells, AaCSS is predominantly localized in the endoplasmic reticulum, but not in the Golgi. Transient functional recombinant expression of wild-type and mutant myc-tagged enzymes in LEC29. Lec32 cells which lack a functional CSS, recombinant expression of His-tagged AaCSS in Escherichia coli	761215	
2.7.7.43	DNA and amino acid sequence determination and analysis, when expressed in mammalian and insect cells, recombinant TcCSS shows in vivo and in vitro CSS activities. In contrast, when expressed in bacteria, it lacks CSS activity because the N-terminal hydrophobic region appears to induce protein aggregation, when expressed in Drosophila S2 cells, TcCSS is predominantly localized in the endoplasmic reticulum, but not in the Golgi. Transient recombinant expression of myc-tagged enzyme in LEC29.Lec32 cells which lack a functional CSS, recombinant expression of His-tagged TcCSS in Escherichia coli	761215	
2.7.7.43	expressed in CHO cells, HeLa cells, and NIH-3T3 cells	671794	
2.7.7.43	expressed in Drosophila S2 cells or LEC29.Lec32 cells	761215	
2.7.7.43	expressed in Escherichia coli and CHO cells	692525	
2.7.7.43	expressed in Escherichia coli Rosetta 2 DE3 cells	760285	
2.7.7.43	expressed in Escherichia coli strain BL21	671567	
2.7.7.43	expressed in Saccharomyces cerevisiae strain Y187	761913	
2.7.7.43	expression in CHO cells	671794	
2.7.7.43	expression in CHO cells or Escherichia coli	645273	
2.7.7.43	expression in Escherichia coli	645268, 645276, 721380	
2.7.7.43	expression in Escherichia coli, enzyme can function in K1 capsular polysaccharide biosynthesis in Escherichia coli	645271	
2.7.7.43	gene Cmas, quantitative PCR expression analysis	760882	
2.7.7.43	high-level expression in Escherichia coli	645266	
2.7.7.43	human CMP-N-acetylneuraminic acid synthetase is expressed in tobacco BY2 suspension-cultured cells, enzyme is demonstrated to be active	671731	
2.7.7.43	the enzyme is subcloned for overexpression in Escherichia coli K12 using the expression vector pKK233-3	645279	
2.7.7.43	the gene is cloned into a T7 expression vector, the protein is expressed in Escherichia coli	645274	
2.7.7.43	the N-terminal domain, residues 39-267, and the C-terminal domain, residues 267-432, of CMP-sialic acid synthetase, and CMP-sialic acid synthetase, residues 39-432, are cloned into a pET22b-Strep vector	705163	
2.7.7.43	transfection of NIH-3T3 and EPC cells	722748	
2.7.7.43	transformation of the CMP-NeuNAc defective Escherichia coli K1 strain EV5 with CMP-NeuNAc synthetase from Neisseria meningitidis can complement the defect in Escherichia coli	645259