Mouse Anti-ACLY Recombinant Antibody (V2-631896) (CBMAB-CA080LY)

Name: Mouse Anti-ACLY Recombinant Antibody (V2-631896)
SKU: CBMAB-CA080LY
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

V2-631896

Application

ELISA, WB, ICC, FC

Immunogen

Recombinant fragment, corresponding to amino acids 734aa-983aa of Human ACLY (C-terminus).

Specificity

Human, Mouse, Rat, Pig

Antibody Isotype

IgG2a

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1:500-1:5,000
IF(ICC)	1:50-1:200

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

Format

Liquid

Buffer

0.1M Tris-Glycine, pH 7.4, 50% glycerol

Preservative

0.2% 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 freezethaw cycles.

More Infomation

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

Human	47
Mouse	708501
Rat	24159
Pig	100125957

UniProt ID

Human	P53396
Mouse	Q91V92
Rat	P16638
Pig	F1S0N2

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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Isotype control

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

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