fbaA Protein, Shigella flexneri (His)

The fbaA protein plays a critical role in cellular metabolism by catalyzing the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerol phosphate) with glyceraldehyde 3-phosphate (G3P), leading to the formation of fructose 1,6-bisphosphate (FBP) role. This enzyme activity is essential for gluconeogenesis and glycolysis, reflecting its involvement in the conversion of key intermediates necessary for energy production and carbon flux. fbaA Protein, Shigella flexneri (His) is the recombinant fbaA protein, expressed by E. coli , with N-6*His labeled tag. The total length of fbaA Protein, Shigella flexneri (His) is 359 a.a., .

The fbaA protein is an enzyme that catalyzes the crucial aldol condensation reaction in both gluconeogenesis and glycolysis. Specifically, it facilitates the condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P), leading to the formation of fructose 1,6-bisphosphate (FBP). This reversible reaction is central to the interconversion of metabolites between glycolysis and gluconeogenesis, playing a pivotal role in cellular energy metabolism. The fbaA enzyme's ability to regulate the conversion of key phosphorylated intermediates highlights its significance in maintaining the balance of glucose production and utilization within the cell. It has to emphasize fbaA's role in this essential biochemical pathway, underlining its importance in cellular energy homeostasis.

Others

E. coli

N-6*His

P0AB73 (M1-L359)

1025905

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.