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ApoA-IV (show APOA4 Proteins) colocalizes with NR4A1 (show NR4A1 Proteins), which suppresses G6Pase (show G6PC Proteins) and PEPCK (show PEPCK Proteins) gene expression at the transcriptional level, reducing hepatic glucose output and lowering blood glucose.
Results indicate that PEPCK promotes tumor growth by increasing glucose and glutamine metabolism, increases anabolic metabolism and promotes mTORC1 activity.
Mitochondrial PCK2 (show PEPCK Proteins) regulates metabolic adaptation and enables glucose-independent tumor growth in various neoplasms.
When autophagy was blocked, the level of glucose-6-phosphatase (G6Pase (show G6PC Proteins)) and phosphoenolpyruvate carboxykinase (PEPCK (show PEPCK Proteins)) was reduced in HepG2 cells and not in Hep3B cells.
PEPCK (show PEPCK Proteins) activity was elevated threefold in lung cancer samples over normal lungs and its activation mediates an adaptive response to glucose depletion in lung cancer.
Amino acid limitation and ER stress inducers, conditions that activate the amino acid response (AAR) and the unfolded protein response (UPR), stimulate PCK2 (show PEPCK Proteins) gene transcription in tumor cell lines.
Expression of phosphoenolpyruvate carboxykinase (show PEPCK Proteins) linked to chemoradiation susceptibility of human colon cancer cells.
expression of HCV nonstructural component NS5A in Huh7 or primary hepatocytes stimulated PEPCK (show PEPCK Proteins) gene expression and glucose output in HepG2 cells.
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
Endoplasmic reticulum stress triggers suppression of AMPK (show PRKAA1 Proteins) while increasing C/EBPbeta (show CEBPB Proteins) and pCREB expression which activates PEPCK (show PEPCK Proteins) gene transcription.
Lactate maintains/induces populations of postnatal neuronal progenitors/neural stem cells in a PEPCK-M (show PEPCK Proteins)-dependent manner
PEPCK-M expression partially rescued defects in lipid metabolism, gluconeogenesis and TCA cycle function impaired by PEPCK-C deletion, while approximately 10% re-expression of PEPCK-C normalized most parameters.
Data show that PEPCK-M (show PEPCK Proteins) message and protein were detected in islets.
Concurrent binding and modifications of AUF1 (show HNRNPD Proteins) and HuR (show ELAVL1 Proteins) mediate the pH-responsive stabilization of phosphoenolpyruvate carboxykinase (show PEPCK Proteins) mRNA in kidney cells.
Transition to lactation does not alter expression of the mitochondrial form of PEPCK (show PEPCK Proteins).
This gene encodes a member of the phosphoenolpyruvate carboxykinase (GTP) family. The protein is a mitochondrial enzyme that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the presence of GTP. A cytosolic form encoded by a different gene has also been characterized and is the key enzyme of gluconeogenesis in the liver. The encoded protein may serve a similar function, although it is constitutively expressed and not modulated by hormones such as glucagon and insulin that regulate the cytosolic form. Alternatively spliced transcript variants have been described.
, phosphoenolpyruvate carboxykinase [GTP], mitochondrial
, phosphoenolpyruvate carboxylase
, phosphopyruvate carboxylase