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anti-Human PFKFB2 Antikörper:
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Human Polyclonal PFKFB2 Primary Antibody für IHC (p), WB - ABIN392769
Yalcin, Clem, Simmons, Lane, Nelson, Clem, Brock, Siow, Wattenberg, Telang, Chesney: Nuclear targeting of 6-phosphofructo-2-kinase (PFKFB3) increases proliferation via cyclin-dependent kinases. in The Journal of biological chemistry 2009
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Chicken Polyclonal PFKFB2 Primary Antibody für WB - ABIN611038
Cherney, McBride, Chen, Alkhatib, Bhatia, Hensley, Smulson: cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase. in Proceedings of the National Academy of Sciences of the United States of America 1988
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Bat Polyclonal PFKFB2 Primary Antibody für WB - ABIN611039
Duriez, Shah: Cleavage of poly(ADP-ribose) polymerase: a sensitive parameter to study cell death. in Biochemistry and cell biology = Biochimie et biologie cellulaire 1998
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Human Polyclonal PFKFB2 Primary Antibody für IHC (p), ELISA - ABIN544944
Soejima, Kawamoto, Akai, Miyoshi, Arai, Morohka, Matsuo, Niikawa, Kimura, Okubo, Mukai: Isolation of novel heart-specific genes using the BodyMap database. in Genomics 2001
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Cow (Bovine) Polyclonal PFKFB2 Primary Antibody für ELISA - ABIN4344993
Arden, Hampson, Huang, Shaw, Aldibbiat, Holliman, Manas, Khan, Lange, Agius: A role for PFK-2/FBPase-2, as distinct from fructose 2,6-bisphosphate, in regulation of insulin secretion in pancreatic beta-cells. in The Biochemical journal 2008
Human Polyclonal PFKFB2 Primary Antibody für WB - ABIN6243012
Novellasdemunt, Tato, Navarro-Sabate, Ruiz-Meana, Méndez-Lucas, Perales, Garcia-Dorado, Ventura, Bartrons, Rosa: Akt-dependent activation of the heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) isoenzyme by amino acids. in The Journal of biological chemistry 2013
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
In diabetes mellitus type 1 loss of myocardial PFK-2 content as a result of reduced insulin signaling impairs the capacity to dynamically regulate glycolysis and elevates the levels of early glycolytic intermediates.
he dysfunction at disease onset was accompanied by increased expression of the rate-limiting glycolytic enzyme phosphofructokinase-2 in activated astrocytes, and by selective reduction in spinal mitochondrial complex I activity
SGK3 is not required for insulin-induced PFK-2 activation and that this effect is likely mediated by PKBalpha.
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 secretion through regulation of glucokinase 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