Alexa Fluor® 488 Anti-PFKFB3 antibody [EPR12594]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

PFKFB3 also known as 6-phosphofructo-2-kinase/fructose-26-bisphosphatase 3 serves a significant role in regulating glycolysis. This bifunctional enzyme weighs approximately 58 kDa and manages levels of fructose-26-bisphosphate a potent activator of another enzyme called phosphofructokinase-1. PFKFB3 expression occurs in various tissues but is especially high in areas with active cell proliferation like the brain and tumors. This enzyme's activity affects glycolytic flux critical for energy production and biosynthesis especially under conditions requiring rapid energy supply.

Biological function summary

PFKFB3 regulates cellular energy metabolism serving as a switch for converting carbohydrates into energy and building blocks for growth. This enzyme is part of a glycolytic complex coordinating energy needs during proliferation and survival. Its activity is important in processes demanding increased energy and anabolic precursors such as cell division. The enzyme's modulation affects fructose-26-bisphosphate levels influencing cellular responses to stress and nutrient availability directly impacting metabolic adaptation.

Pathways

PFKFB3 integrates into the glycolytic pathway and the pentose phosphate pathway. PFKFB3's control over fructose-26-bisphosphate levels influences phosphofructokinase-1 modulating the glycolytic pathway's rate. This modulation impacts energy production efficiency and the provision of metabolites required for nucleotide synthesis linking to the pentose phosphate pathway. Proline-rich AKT substrate of 40 kDa (PRAS40) and AKT may also interact indirectly to regulate PFKFB3 activity in these metabolic pathways.

Associated diseases and disorders

PFKFB3 links strongly to cancer and diabetes. Its upregulation in cancerous tissues supports tumor growth by promoting glycolysis known as the Warburg effect. Cancer-associated proteins such as KRAS often rely on PFKFB3's glycolytic control to sustain proliferative signaling. Additionally in diabetes altered PFKFB3 activity can contribute to insulin resistance due to disrupted metabolic homeostasis with insulin pathway proteins like IRS1 potentially interacting with it in this context.