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UCA1/miR-182/PFKFB2 axis modulates chemokine CXCL14 secretion, glycolysis and invasion of glioma cells in glioblastoma-associated stromal cells .
Crystal structure of human and cattle heart PFKFB2 and the inhibitory influence of citrate on substrate binding has been described.
Variation in PFKFB2 appears to reduce PFKFB2 expression in adipose and kidney tissues, and thereby increase risk for adiposity and diabetic nephropathy.
Highly expressed PFKFB2 protein is associated with hepatocellular carcinoma.
bifunctionality of PFK-2/FBPase-2 complements the metabolic zonation of the liver by ensuring coherent switching in response to insulin and glucagon.
amino acids stimulate Fru-2,6-P2 synthesis by Akt-dependent PFKFB2 phosphorylation and activation and show how signaling and metabolism are inextricably linked.
A persistent increase in 6-phosphofructo-2-kinase produced by a change in PFK-2/FBPase-2 isoform expression that may play an important role in the regulation of muscle glycolysis.
Suggest that PFKFB2 is not an essential upstream regulator of the anti-leukemic effects of glucocorticoids.
induction of de novo lipid synthesis by androgen requires transcriptional up-regulation of HK2 and PFKFB2, and phosphorylation of PFKFB2 generated by the PI3K/Akt signal pathway to supply the source for lipogenesis from glucose in prostate cancer cells.
Human islets expressed the PFKFB2 and PFKFB3 isoforms. PFK-2/FBPase-2 protein rather than its product fructose 2,6-P(2) is the over-riding determinant of glucose-induced insulin secretion through regulation of glucokinase activity
SGK3 is not required for insulin-induced PFK-2 activation and that this effect is likely mediated by PKBalpha.
The protein encoded by this gene is involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls glycolysis in eukaryotes. The encoded protein has a 6-phosphofructo-2-kinase activity that catalyzes the synthesis of fructose-2,6-bisphosphate, and a fructose-2,6-biphosphatase activity that catalyzes the degradation of fructose-2,6-bisphosphate. This protein regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle. This enzyme functions as a homodimer. Two transcript variants encoding two different isoforms have been found for this gene.
, 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2-like
, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
, 6PF-2-K/Fru-2,6-P2ASE heart-type isozyme
, 6PF-2-K/Fru-2,6-P2ase 2
, PFK/FBPase 2
, PFKFB, cardiac
, fructose-2,6-bisphosphatase, cardiac isozyme
, 6PF-2-K/Fru-2,6-P2ase heart-type isozyme
, PFK-2/FBPase-2 gene B
, 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (heart)
, fructose 6-phosphate 2-kinase/fructose 2,6-bisphosphatase
, 6-phosphofructo-2-kinase /fructose-2,6-bisphosphatase