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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 (22) and ACLY Proteins (4) and many more products for this protein.
Showing 10 out of 125 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 Pubmed References
Cow (Bovine) Polyclonal ACLY Primary Antibody for IHC, WB - ABIN2775558
Infantino, Iacobazzi, Palmieri, Menga: ATP-citrate lyase is essential for macrophage inflammatory response. in Biochemical and biophysical research communications 2013
Cow (Bovine) Polyclonal ACLY Primary Antibody for WB - ABIN2773810
Convertini, Menga, Andria, Scala, Santarsiero, Castiglione Morelli, Iacobazzi, Infantino: The contribution of the citrate pathway to oxidative stress in Down syndrome. in Immunology 2016
ACLY facilitates histone acetylation at double-strand break (DSB) sites, impairing 53BP1 localization and enabling BRCA1 recruitment and DNA repair by homologous recombination. ACLY phosphorylation and nuclear localization are necessary for its role in promoting BRCA1 recruitment.
The protein crystallized consisted of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. (2S,3S)-2-Hydroxycitrate binds in the same orientation as citrate, but the citrate-binding domain (residues 248-421) adopts a different orientation with respect to the rest of the protein (residues 4-247, 490-746 and 748-809) from that previously seen.
CUL3 (show CUL3 Antibodies) interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells
we found that depletion of ATP citrate lyase suppressed tumor growth, which suggests that ATP citrate lyase-related inhibitors might be potential therapeutic approaches for breast cancer.
Results show that ACLY is a key phosphoprotein effector of IL-2 (show IL2 Antibodies)-mediated T-cell responses. ACLY becomes phosphorylated on serine 455 in T lymphocytes upon IL-2 (show IL2 Antibodies)-driven activation of AKT (show AKT1 Antibodies), and depletion or inactivation of ACLY compromises IL-2 (show IL2 Antibodies)-promoted T-cell growth.
ACLY was also required for LMW-E-mediated transformation, migration, and invasion of breast cancer cells in vitro along with tumor growth in vivo In clinical specimens of breast cancer, the absence of LMW-E and low expression of adipophilin (PLIN2 (show PLIN2 Antibodies)), a marker of lipid droplet formation, associated with favorable prognosis
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.
ACL (show APOC4 Antibodies) plays a critical role in epigenetic regulation of diabetic renal fibrosis.
ATP-citrate lyase inhibitor bempedoic acid effectively prevents plasma and tissue lipid elevations and attenuates the onset of inflammation, leading to the prevention of atherosclerotic lesion development in a Ldlr (show LDLR Antibodies) knockout mouse model of metabolic dysregulation.
IL-4 (show IL4 Antibodies) signaling co-opts the Akt (show AKT1 Antibodies)-mTORC1 pathway to regulate Acly, a key enzyme in acetyl-CoA (show LPCAT1 Antibodies) synthesis, leading to increased histone acetylation and macrophage gene induction.
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).
we identified three non-synonymous mutations in ACLY exons in five beef cattle populations. Single nucleotide polymorphism (SNP) g.17127C>T is significantly associated with chest girth and body height, and with body slanting length. SNP g.40427T>C is significantly associated with an increase in chest girth. ACLY gene are associated with growth traits in beef cattle in northwest China
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