PFKFB3 Protein, Human (sf9, His-GST)

The PFKFB3 protein is a key player in cellular energy metabolism as it exerts dual functions by catalyzing the synthesis and degradation of fructose 2,6-bisphosphate (F-2,6-BP). F-2,6-BP is an important allosteric regulator of glycolysis, controlling glucose utilization for energy production. PFKFB3 Protein, Human (sf9, His-GST) is the recombinant human-derived PFKFB3 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.

PFKFB3 protein is a key player in cellular energy metabolism as it serves a dual function by catalyzing both the synthesis and degradation of fructose 2,6-bisphosphate (F-2,6-BP). F-2,6-BP is a crucial allosteric regulator of glycolysis, exerting control over the rate of glucose utilization for energy production. PFKFB3 acts as a kinase to generate F-2,6-BP, promoting the activation of phosphofructokinase-1 (PFK-1), a rate-limiting enzyme in glycolysis. This results in enhanced glycolytic flux and increased energy production. Conversely, PFKFB3 can also act as a phosphatase to degrade F-2,6-BP, exerting inhibitory effects on PFK-1 and subsequently slowing down glycolysis. The tight regulation of PFKFB3 activity is crucial for maintaining cellular energy homeostasis and has implications in various physiological and pathological processes, including cancer and metabolic disorders. Understanding the intricate regulatory mechanisms governing PFKFB3 can provide insights into therapeutic strategies targeting glycolytic metabolism.

Human

Sf9 insect cells

N-His;N-GST

Q16875-1 (M1-H520)

5209  [NCBI]

Approximately 75 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.