Western blot (WB) analysis of PFKFB1/4 (E349) pAb in extracts from HeLa cells.
Theoretical MW
54 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
PFKFB (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase) is a bifunctional enzyme, having both kinase and phosphatase activities residing on the same enzyme subunit but having distinct active sites. PFKFB regulates the steady-state concentration of fructose-2,6-bisphosphate, a potent activator of a key regulatory enzyme of glycolysis, phosphofructokinase. To date, four PFKFB isozymes (PFKFB 1-4) have been described, which show differences in their tissue distribution and kinetic properties in response to allosteric effectors and hormonal signals. Among the PFKFB's PFKFB3 has the highest kinase:phosphatase ratio, in part because it lacks the characteristic serine phosphorylation site near the N-terminal that down-modulates kinase activity. PFKFB3 was first described in the rapidly growing placenta. The glucolitic rate in placenta is accelerated by anoxia and by maternal diabetes. Cancer cells maintain a high glycolytic rate even in the presence of oxygen, a phenomenon known as the Warburg effect. The glycolytic rate in the placenta, another fast-growing tissue, is accelerated by anoxia and by maternal diabetes.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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