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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 (show INS Proteins) and glucagon (show GCG Proteins).
amino acids stimulate Fru-2,6-P2 synthesis by Akt (show AKT1 Proteins)-dependent PFKFB2 phosphorylation and activation and show how signaling and metabolism are inextricably linked.
A persistent increase in 6-phosphofructo-2-kinase (show PFKFB3 Proteins) 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 (show HK2 Proteins) and PFKFB2, and phosphorylation of PFKFB2 generated by the PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) 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 i (show INS Proteins)nsulin secretion through regulation of gluco (show GCK Proteins)kinase activity
SGK3 (show SGK3 Proteins) is not required for insulin (show INS Proteins)-induced PFK-2 activation and that this effect is likely mediated by PKBalpha (show AKT1 Proteins).
Our results demonstrate that in diet-induced obesity, high Fru-2,6-P2 levels in transgenic livers caused changes in hepatic gene expression profiles for key gluconeogenic and lipogenic enzymes.
mouse islets expressed PFKFB2 at the mRNA level; PFK-2/FBPase-2 protein rather than its product fructose 2,6-P(2) is the over-riding determinant of glucose-induced insulin (show INS Proteins) secretion through regulation of glucokinase (show GCK Proteins) activity or subcellular targeting.
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