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Mouse Anti-ACLY Recombinant Antibody (V2-630606) (CBMAB-BR003LY)

The product is antibody recognizes ACLY. The antibody 5I2 immunoassay techniques such as: FC, IHC-P, WB.
See all ACLY antibodies
Published Data
Mouse Anti-ACLY Recombinant Antibody (5I2) (CBMAB-BR003LY) in WB
Western blot analysis of ACL. ...View More
Huang, Y., Zhao, C., Kong, Y., Tan, P., Liu, S., Liu, Y., ... & Wang, J. (2021). Elucidation of the mechanism of NEFA-induced PERK-eIF2α signaling pathway regulation of lipid metabolism in bovine hepatocytes. The Journal of Steroid Biochemistry and Molecular Biology, 211, 105893.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
V2-630606
Antibody Isotype
IgG2b
Application
FC: 1-3 μg/1x10 cells, IHC-P: 0.5-1 μg/ml, WB: 0.1-0.5 μg/ml

Basic Information

Immunogen
E. coli-derived human ATP citrate lyase recombinant protein.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
FC1-3 µg/10^6 cells
IF(ICC)2 µg/ml
WB0.1-0.5 µg/ml
IHC-P0.5-1 µg/ml

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized
Buffer
Trehalose, 0.9mg NaCl, 0.2mg Na2HPO4
Preservative
0.05% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
ATP Citrate Lyase
Introduction
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. Multiple transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Dec 2014]
Entrez Gene ID
Human47
Mouse708501
Rat24159
UniProt ID
HumanP53396
MouseQ91V92
RatP16638
Alternative Names
ATP-citrate synthase; ATP-citrate (pro-S-)-lyase; ACL; Citrate cleavage enzyme; ACLY
Function
Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.
Biological Process
Acetyl-CoA biosynthetic process
Cholesterol biosynthetic process
Citrate metabolic process
Coenzyme A metabolic process
Fatty acid biosynthetic process
Fatty-acyl-CoA biosynthetic process
Lipid biosynthetic process
Neutrophil degranulation
Oxaloacetate metabolic process
Positive regulation of cellular metabolic process
Cellular Location
Cytosol
PTM
Phosphorylated by PKA and GSK3 in a sequential manner; phosphorylation results in activation of its activity. Phosphorylation on Thr-447 and Ser-451 depends on the phosphorylation state of Ser-455 (By similarity). Phosphorylation on Ser-455 is decreased by prior phosphorylation on the other 2 residues (By similarity).
ISGylated.
Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF. Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites. Acetylation promotes de novo lipid synthesis. Deacetylated by SIRT2.
Ubiquitinated at Lys-540, Lys-546 and Lys-554 by UBR4, leading to its degradation. Ubiquitination is probably inhibited by acetylation at same site (Probable).

Dominguez, M., Brüne, B., & Namgaladze, D. (2021). Exploring the Role of ATP-Citrate Lyase in the Immune System. Frontiers in Immunology, 12, 14.

Han, Q., Chen, C. A., Yang, W., Liang, D., Lv, H. W., Lv, G. S., ... & Wang, H. Y. (2020). ATP-citrate lyase regulates stemness and metastasis in hepatocellular carcinoma via the Wnt/β-catenin signaling pathway. Hepatobiliary & Pancreatic Diseases International.

Feng, X., Zhang, L., Xu, S., & Shen, A. Z. (2020). ATP-citrate lyase (ACLY) in lipid metabolism and atherosclerosis: an updated review. Progress in lipid research, 77, 101006.

Icard, P., Wu, Z., Fournel, L., Coquerel, A., Lincet, H., & Alifano, M. (2020). ATP citrate lyase: a central metabolic enzyme in cancer. Cancer letters, 471, 125-134.

Kumari, R., Deshmukh, R. S., & Das, S. (2019). Caspase-10 inhibits ATP-citrate lyase-mediated metabolic and epigenetic reprogramming to suppress tumorigenesis. Nature communications, 10(1), 1-15.

Göttgens, E. L., van den Heuvel, C. N., de Jong, M. C., Kaanders, J. H., Leenders, W. P., Ansems, M., ... & Span, P. N. (2019). ACLY (ATP citrate lyase) mediates radioresistance in head and neck squamous cell carcinomas and is a novel predictive radiotherapy biomarker. Cancers, 11(12), 1971.

Wei, J., Leit, S., Kuai, J., Therrien, E., Rafi, S., Harwood, H. J., ... & Tong, L. (2019). An allosteric mechanism for potent inhibition of human ATP-citrate lyase. Nature, 568(7753), 566-570.

Granchi, C. (2018). ATP citrate lyase (ACLY) inhibitors: An anti-cancer strategy at the crossroads of glucose and lipid metabolism. European journal of medicinal chemistry, 157, 1276-1291.

Namgaladze, D., Zukunft, S., Schnütgen, F., Kurrle, N., Fleming, I., Fuhrmann, D., & Brüne, B. (2018). Polarization of human macrophages by interleukin-4 does not require ATP-citrate lyase. Frontiers in immunology, 9, 2858.

Teng, L., Chen, Y., Cao, Y., Wang, W., Xu, Y., Wang, Y., ... & Su, Y. (2018). Overexpression of ATP citrate lyase in renal cell carcinoma tissues and its effect on the human renal carcinoma cells in vitro. Oncology letters, 15(5), 6967-6974.

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For research use only. Not intended for any clinical use.

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