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AB235007

Recombinant Human ATP citrate lyase protein (His tag)

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Recombinant Human ATP citrate lyase protein (His tag) is a Human Fragment protein, in the 4 to 265 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

ATP-citrate synthase, ATP-citrate (pro-S-)-lyase, Citrate cleavage enzyme, ACL, ACLY

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SDS-PAGE - Recombinant Human ATP citrate lyase protein (His tag) (AB235007)
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Supplier Data

SDS-PAGE - Recombinant Human ATP citrate lyase protein (His tag) (AB235007)

ab235007 analyzed by (Tris-Glycine gel) discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

6x His tag N-Terminus SUMO tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P53396

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

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Complementary Products

Primary Antibodies

AB40793

Anti-ATP citrate lyase antibody [EP704Y]

RabMAb|Recombinant|KO Validated|20ul selling size

Flow Cytometry (Intracellular) - Anti-ATP citrate lyase antibody [EP704Y] (AB40793)

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Proteins & Peptides

AB195163

Recombinant Human ZMYND8 protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human ZMYND8 protein (GST tag N-Terminus) (AB195163)

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Proteins & Peptides

AB313361

Recombinant Human WFDC2 Protein (His tag)

Mass Spectrometry - Recombinant Human WFDC2 Protein (His tag) (AB313361)

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Proteins & Peptides

AB217407

Recombinant human Vitronectin/S-Protein (Animal Free)

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  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"linker":null,"sequence":"KAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLK","proteinLength":"Fragment","predictedMolecularWeight":"45.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":265,"aminoAcidStart":4,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P53396","tags":[{"tag":"6x His","terminus":"N-Terminus"},{"tag":"SUMO","terminus":"N-Terminus"}]}]
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Properties and storage information

Form
Liquid
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ATP citrate lyase (ACL ACLY) is an enzyme responsible for converting citrate and coenzyme A into acetyl-CoA and oxaloacetate using ATP in the process. This reaction is key for lipid and cholesterol biosynthesis. ACLY's alternate name is ATP citrate (pro-S)-lyase and it has a molecular weight of approximately 120 kDa. The enzyme is expressed mainly in the cytoplasm with substantial amounts found in liver and adipose tissues.
Biological function summary

ATP citrate lyase plays an important role in lipid metabolism and energy production. It drives the conversion of citrate-derived acetyl-CoA a central metabolite in lipogenesis providing substrates for fatty acid and cholesterol synthesis. ACLY functions as a homotetramer complex to facilitate its enzymatic activity. This mechanism supports energy homeostasis linking carbohydrate metabolism with lipid biosynthesis.

Pathways

The enzyme ATP citrate lyase is instrumental in the citric acid cycle and fatty acid synthesis pathways. It is a central player in the cholesterol biosynthesis pathway which tightly connects to acetyl-CoA and citrate shuttle processes. In these pathways it interacts functionally with other enzymes such as acetyl-CoA carboxylase which further processes acetyl-CoA into malonyl-CoA serving as a precursor for fatty acid elongation.

ATP citrate lyase becomes significant in metabolic syndrome and cancer. Elevated expression and activity are linked to an increased risk of metabolic diseases including obesity and type 2 diabetes due to its role in excessive lipid accumulation. Moreover cancer cells often exhibit upregulated ACLY activity encouraging tumor growth by supplying acetyl-CoA for lipid biosynthesis. Its activity is intricately linked to proteins such as fatty acid synthase which also contribute to altered lipid profiles in these conditions.
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General info

Function

Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism.

Sequence similarities

In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.. In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.

Post-translational modifications

Phosphorylated by PKA and GSK3 in a sequential manner; phosphorylation results in activation of its activity (PubMed:10653665). 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). Phosphorylated at Ser-455 by BCKDK and dephosphorylated by protein phosphatase PPM1K.. ISGylated.. Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF (PubMed:23932781). Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites (PubMed:23932781). Acetylation promotes de novo lipid synthesis (PubMed:23932781). Deacetylated by SIRT2.. Benzoylated at Lys-978 (PubMed:39524354). Debenzoylated by SIRT3; inhibiting the ATP-citrate synthase activity (PubMed:39524354).. Ubiquitinated at Lys-540, Lys-546 and Lys-554 by the BCR(KLHL25) E3 ubiquitin ligase complex and UBR4, leading to its degradation (PubMed:23932781, PubMed:27664236, PubMed:34491895). Ubiquitination is probably inhibited by acetylation at same site (PubMed:23932781). BCR(KLHL25)-mediated degradation of ACLY promotes fatty acid oxidation and is required for differentiation of inducible regulatory T (iTreg) cells (PubMed:34491895).

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Product protocols

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Target data

Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism.
See full target information ATP-citrate synthase
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Product promise

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