BD-PB4028

PFKFB3 Rabbit Polyclonal Antibody (N-term)

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

常规抗体

WB

Human, Mouse

NP_001138915.1;NP_004557.1

Q16875

This PFKFB3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human PFKFB3.

WB~~1:1000;IHC-P~~1:100~500

60kDa

Rabbit IgG

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.

Ubiquitous.

现货