Anti-PFKFB3 Antibody, clone 4C10.2 clone 4C10.2, from mouse

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (EC 2.7.1.105; EC 3.1.3.46; UniProt Q16875; also known as 6PF-2-K/Fru-2,6-P2ase 3, 6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme, iPFK-2, PFK/FBPase 3, Renal carcinoma antigen NY-REN-56) is encoded by the PFKFB3 gene (Gene ID 5209) in human. The homodimeric bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFBs) phosphorylate fructose 6-phosphate (F6P) to fructose-2,6-bisphosphate (F2,6BP), which in turn activates 6-phosphofructo-1-kinase and glycolytic flux to lactate. PFKFB3 is distinguished from the other three known PFKFBs (PFKFB1, 2, 4) by the presence of multiple copies of the AUUUA instability motif in its 3′-untranslated region, a very high kinase:phosphatase activity ratio (740:1), increased protein expression in rapidly proliferating transformed cells, solid tumors and leukemias, and regulation by several proteins essential for tumor progression. Heterozygous deletion results in reduced glucose metabolism and growth of Ras-transformed tumors in Pfkfb3+/- mice. PFKFB3 nuclear localization is reported in multiple cell lines due to the presence of a highly conserved C-terminal nuclear localization motif. F2,6BP is reported to enhance cyclin-dependent kinase (Cdk) activity toward p27 Thr187 phosphorylation in vitro, while ectopic expression of PFKFB3 in the nucleus is found to stimulate cellular proliferation without affecting glycolysis, suggesting a novel role of PFKFB3-mediated F2,6BP in cell cycle regulation. The canonical form of human PFKFB3 is a 520-a.a. protein composed of an N-terminal 6-phosphofructo-2-kinase domain (a.a. 1-245) and a C-terminal fructose-2,6-bisphosphatase domain (a.a. 246-520).