PFKFB3 Antibody (N-term) Blocking Peptide

Provided below are standard protocols that you may find useful for product applications.

Background

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.

References

Navarro-Sabate, A., et al., Gene 264(1):131-138 (2001).Chesney, J., et al., Proc. Natl. Acad. Sci. U.S.A. 96(6):3047-3052 (1999).Sakakibara, R., et al., J. Biochem. 122(1):122-128 (1997).Hamilton, J.A., et al., Mol. Endocrinol. 11(4):490-502 (1997).Sakai, A., et al., J. Biochem. 119(3):506-511 (1996).