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Rabbit Anti-ACLY Recombinant Antibody (V2-179319) (CBMAB-A0615-YC)

Provided herein is a Rabbit monoclonal antibody against Human ATP Citrate Lyase. The antibody can be used for immunoassay techniques, such as ICC, IF.
See all ACLY antibodies
Published Data

Summary

Host Animal
Rabbit
Specificity
Human
Clone
V2-179319
Antibody Isotype
IgG
Application
ICC, IF

Basic Information

Immunogen
Synthetic peptide. This information is proprietary to Abcam and/or its suppliers.
(Peptide available as ab207504)
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
FC1:30
IF(ICC)1:50
WB1:10,000
IP1:20

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

Buffer
PBS, pH7.2, 0.05% BSA, 40% Glycerol
Preservative
0.01% sodium azide
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw 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 acety
Entrez Gene ID
UniProt ID
Alternative Names
ATP Citrate Lyase; ATP-Citrate (Pro-S-)-Lyase; Citrate Cleavage Enzyme; EC 2.3.3.8; ACL; ATP Citrate Synthase; ATP-Citrate Synthase; ATPCL; CLATP;
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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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