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PFKFB3 Antibody (N-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession Q16875
Clone Names 3051407
Peptide ID 3051407
Additional Information
Gene ID 5209
Other Names 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 3, 6PF-2-K/Fru-2, 6-P2ase 3, PFK/FBPase 3, 6PF-2-K/Fru-2, 6-P2ase brain/placenta-type isozyme, Renal carcinoma antigen NY-REN-56, iPFK-2, 6-phosphofructo-2-kinase, Fructose-2, 6-bisphosphatase, PFKFB3
Target/Specificity The synthetic peptide sequence used to generate the antibody AP8145a was selected from the N-term region of human PFKFB3 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Function Synthesis and degradation of fructose 2,6-bisphosphate.
Tissue Location Ubiquitous.
Research Areas
Citations (0)

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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.


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).

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$ 99.00
Cat# BP8145a
Availability: In Stock
Bulk Size
Seasonal Special on Bulk Order
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