Human Recombinant ACLY protein, His Tag (V2LY-0526-LY2199)

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Basic Information

Expressed Host
Baculovirus-Insect Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant ACLY protein, His Tag consist of Amino Acid: 1-1101 and predicts a molecular mass of 123 kDa.
Molecule Mass
123 kDa
Sequence
Amino Acid: 1-1101
Species
Human

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

Purity
>85% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Liquid
Buffer
PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
ATP Citrate Lyase
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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