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ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Additionally we are shipping ACLY Kits (13) and ACLY Proteins (4) and many more products for this protein.
Showing 10 out of 89 products:
Human Monoclonal ACLY Primary Antibody for ICC, FACS - ABIN1098143
Chu, Lin, Hendel, Kulpa, Brownsey, Johnson: ATP-citrate lyase reduction mediates palmitate-induced apoptosis in pancreatic beta cells. in The Journal of biological chemistry 2010
Show all 2 references for ABIN1098143
Human Polyclonal ACLY Primary Antibody for WB - ABIN2775558
Infantino, Iacobazzi, Palmieri, Menga: ATP-citrate lyase is essential for macrophage inflammatory response. in Biochemical and biophysical research communications 2013
ACC1 (show ACACA Antibodies) and ACLY regulate the levels of ETV4 (show ETV4 Antibodies) under hypoxia via increased alpha-ketoglutarate. These results reveal that the ACC1 (show ACACA Antibodies)/ACLY-alpha-ketoglutarate-ETV4 (show ETV4 Antibodies) axis is a novel means by which metabolic states regulate transcriptional output
ACL activity is associated with increased ATP. Activation of this IGF1 (show IGF1 Antibodies)/ACL/cardiolipin pathway combines anabolic signaling with induction of mechanisms needed to provide required ATP.
These results suggest that the combined expression of GLUT1 (show SLC2A1 Antibodies) and ACLY could be a more valuable prognostic factor than their individual expression in node-negative patients with NSCLC.
Polymorphisms of ATP citrate lyase gene is associated with recurrence in colorectal cancer.
SNP rs9912300 in ACLY gene was significantly associated with response to therapy in hepatocellular carcinoma
The activation of AMPK (show PRKAA1 Antibodies) under ACLY knockdown conditions may lead to p53 (show TP53 Antibodies) activation, ultimately leading to cellular senescence.
ATP citrate lyase mediates resistance of colorectal cancer cells to SN38.
These data indicate that inhibition of ACLY might affect both fatty acid elongation in ER and FAO in mitochondria, thereby explaining the TG accumulation with altered fatty acid composition.
ACLY inhibition exerts an anticancer effect via increased reactive oxygen species, and p-AMPK (show PRKAA1 Antibodies) could be a predictive biomarker for its therapeutic outcome.
Single nucleotide polymorphisms in the ACACA (show ACACA Antibodies) and ACLY genes are associated with a relative change in plasma triglycierides following fish oil supplementation.
These data demonstrate that ACLY mediates glucose-dependent de novo lipogenesis in response to LPS (show TLR4 Antibodies) signaling and identify a role for ACLY in several phenotypic changes that define plasma cell differentiation
Results suggest a role for DNA methyltransferase 1 (DNMT1 (show DNMT1 Antibodies)) in modulating the timing of differentiation and describe a novel ATP-citrate lyase (ACL)-miR (show MLXIP Antibodies)-148a-dependent mechanism for regulating DNMT1 (show DNMT1 Antibodies) during adipogenesis.
Differences between human and rodent pancreatic islets: low pyruvate carboxylase (show PC Antibodies), atp citrate lyase, and pyruvate carboxylation and high glucose-stimulated acetoacetate in human pancreatic islets.
Results demonstrate that hepatic ATP-citrate lyase suppression exerts profound effects on triglyceride mobilization as well as fatty acid compositions in the liver, suggesting an important role for ACL (show APOC4 Antibodies) in lipid metabolism.
Data suggest that ATP-citrate lyase (ACLY) expression and activity can be suppressed by exogenous lipids and demonstrate a critical role for ACLY in pancreatic beta cell survival.
crucial role of hepatic ATP-citrate lyase in lipid and glucose metabolism
findings suggest that ATP-citrate lyase activity is required to link growth factor-induced increases in nutrient metabolism to the regulation of histone acetylation and gene expression
The results of this study indicate that a C/T mutation affects ACL mRNA expression, probably via the activator protein 2 (show TFAP2A Antibodies).
ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene.
ATP citrate lyase
, ATP citrate synthase
, ATP-citrate synthase-like
, ATP-citrate lyase
, ATP-citrate synthase
, citrate synthase, mitochondrial
, atp-citrate synthase
, ATP-citrate (pro-S-)-lyase
, citrate cleavage enzyme