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anti-Mouse (Murine) G6PC Antibodies:
anti-Human G6PC Antibodies:
anti-Rat (Rattus) G6PC Antibodies:
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Mouse (Murine) Polyclonal G6PC Primary Antibody for WB - ABIN4894612
Tao, Zhang, Zeng, Shulman, Jin: Niclosamide ethanolamine-induced mild mitochondrial uncoupling improves diabetic symptoms in mice. in Nature medicine 2014
Show all 2 references for ABIN4894612
Human Polyclonal G6PC Primary Antibody for FACS, IHC (p) - ABIN651417
Tu, Bagnall, Duflou, Lynch, Twigg, Semsarian: Post-mortem pathologic and genetic studies in "dead in bed syndrome" cases in type 1 diabetes mellitus. in Human pathology 2010
Show all 2 references for ABIN651417
Cow (Bovine) Polyclonal G6PC Primary Antibody for IHC, WB - ABIN2781770
Iwasa, Kobayashi, Mifuji-Moroka, Hara, Miyachi, Sugimoto, Tanaka, Fujita, Gabazza, Takei: Branched-chain amino acid supplementation reduces oxidative stress and prolongs survival in rats with advanced liver cirrhosis. in PLoS ONE 2013
We conclude that G6PD (show G6PD Antibodies) deficiency at the level of the animals in the present study may not be a risk factor for developing CSN-OT, but this remains to be verified for human subjects
The results strongly suggested that the increase of glucagon (show GCG Antibodies) levels could account for the induction of G6pc expression in the kidneys and intestine of L-G6pc-/- mice.
PPARalpha (show PPARA Antibodies) is responsible for glucose production through the up-regulation of hepatic G6Pase gene expression during fasting or type 2 diabetes animal models
gene transcription in H4IIE cells mediated by hepatocyte nuclear factor-4 (show HNF4A Antibodies) alpha's stimulatory effect of peroxisome proliferator-activated receptor gamma co-activator-1 (show PPARGC1A Antibodies) alpha
Evidence for the expression of the catalytic domain of hepatic glucose-6-phosphatase in pancreatic islets.
Loss of G6pt activity causes neutropenia, and local production of the chemokines KC and macrophage inflammatory protein-2 (show CXCL2 Antibodies) are defective in G6pt-/- neutrophils.
G6pc expression was functionally silenced by adenovirus-mediated delivery of short hairpin RNA.
muscle expresses both Glc-6-Pase-beta and Glc-6-P transporter and that they can couple to form an active Glc-6-Pase complex
Brain contains a functional glucose-6-phosphatase complex capable of endogenous glucose production.
Hippel Lindau tumor suppressor regulates hepatic glucose metabolism by controlling expression of glucose transporter 2 (show SLC2A2 Antibodies) and glucose 6-phosphatase
Post-translational regulation of the glucose-6-phosphatase complex by cyclic AMP (show APRT Antibodies) is a crucial determinant of endogenous glucose production and is controlled by the glucose-6-phosphate transporter (show SLC37A4 Antibodies).
ApoA-IV (show APOA4 Antibodies) colocalizes with NR4A1 (show NR4A1 Antibodies), which suppresses G6Pase and PEPCK (show PEPCK Antibodies) gene expression at the transcriptional level, reducing hepatic glucose output and lowering blood glucose.
By direct DNA sequencing, three novel G6PC variations were identified which expanded the G6PC mutation spectrum, and provided conclusive genetic evidences for the definitive diagnosis of the Chinese patients.
This study is the first to demonstrate a functional relationship between the critical gluconeogenic and glycogenolytic enzyme G6PC with the metabolic adaptations during glioblastoma invasion.
The spectrum of mutations in the G6PC gene.
Lipopolysaccharide and monophosphoryl lipid A also up-regulated G6PC and PCK1 (show PCK1 Antibodies) transcript abundance in a TLR4 (show TLR4 Antibodies)-dependent manner.
LSD1 (show KDM1A Antibodies) regulates transcription activation of two gluconeogenic genes, FBP1 (show FBP1 Antibodies) and G6Pase.
Both GSD-1a and G6PT strongly colocalised in perinuclear membranes. showed that GSD1 mutations did neither alter the G6PC or G6PT chimera localisation, nor the interaction between G6PT termini.
results reveal a novel link between glucose metabolism and the DNA damage signaling pathway and suggest a possible role for PEPCK and G6P in the DNA damage response
data mitigate against G6PD (show G6PD Antibodies) deficiency contributing to stroke risk in individuals with sickle cell anemia.
Glucose-6-phosphatase (G6Pase) is a multi-subunit integral membrane protein of the endoplasmic reticulum that is composed of a catalytic subunit and transporters for G6P, inorganic phosphate, and glucose. This gene (G6PC) is one of the three glucose-6-phosphatase catalytic-subunit-encoding genes in human: G6PC, G6PC2 and G6PC3. Glucose-6-phosphatase catalyzes the hydrolysis of D-glucose 6-phosphate to D-glucose and orthophosphate and is a key enzyme in glucose homeostasis, functioning in gluconeogenesis and glycogenolysis. Mutations in this gene cause glycogen storage disease type I (GSD1). This disease, also known as von Gierke disease, is a metabolic disorder characterized by severe hypoglycemia associated with the accumulation of glycogen and fat in the liver and kidneys.
, glucose-6-phosphatase alpha
, glucose-6-phosphatase, catalytic (glycogen storage disease type I, von Gierke disease)
, glucose-6-phosphatase catalytic subunit