Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

ACLY

Uniprot No.

P53396

Research Area

Metabolism

Alternative Names

ACL; Acly; ACLY_HUMAN; ATP citrate (pro-S) lyase; ATP citrate lyase; ATP citrate synthase; ATP-citrate (pro-S-)-lyase; ATP-citrate synthase; ATPcitrate synthase; ATPCL; Citrate cleavage enzyme; CLATP; OTTHUMP00000164773

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

4-265aa

Target Protein Sequence

KAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLK
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

45.5kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-SUMO-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The expression region of this recombinant Human ACLY covers amino acids 4-265. The calculated molecular weight for this ACLY protein is 45.5 kDa. This ACLY protein is produced using e.coli expression system. The N-terminal 6xHis-SUMO tag was fused into the coding gene segment of ACLY, making it easier to detect and purify the ACLY recombinant protein in the later stages of expression and purification.

ATP-citrate synthase (ACLY) is an important metabolic enzyme involving lipid metabolism and cellular energy balance. In lipid metabolism, ACLY catalyzes the synthesis of acetyl-coenzyme A and citrate within the cell, critical steps in cholesterol synthesis and fatty acid biogenesis. In recent years, researchers have observed overexpression of ACLY in various cancers, particularly malignant tumors like breast cancer. This suggests its significant role in the onset and progression of cancer. One of the most important areas of research is exploring the mechanisms of ACLY in cancer metabolic reprogramming and its potential application as a drug target. What's more, ACLY is involved in regulating lipid-activated receptors and is associated with metabolic disorders such as diabetes.

Target Background

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.

Gene References into Functions

SLC25A1 and ACLY upregulation suggests that metabolic reprogramming in Behcet's syndrome involves the citrate pathway dysregulation. PMID: 30050389
ACL regulates the net amount of acetyl groups available, leading to alterations in acetylation of H3(K9/14) and H3(K27) at the MYOD locus, thus increasing MYOD expression. PMID: 29241530
Results show that ACLY was up-regulated in human gastric cancer (GC) tissues and cell lines and a critical downstream target of the tumor suppressor activity of miR-133b in GC. PMID: 28901466
ACLY and ACSS2 are both activated to produce cytosolic Ac-CoA from glucose carbon for lipogenesis during human cytomegalovirus infection. PMID: 28167750
ACLY facilitates histone acetylation at double-strand break (DSB) sites, impairing 53BP1 localization and enabling BRCA1 recruitment and DNA repair by homologous recombination. ACLY phosphorylation and nuclear localization are necessary for its role in promoting BRCA1 recruitment. PMID: 28689661
The protein crystallized consisted of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. (2S,3S)-2-Hydroxycitrate binds in the same orientation as citrate, but the citrate-binding domain (residues 248-421) adopts a different orientation with respect to the rest of the protein (residues 4-247, 490-746 and 748-809) from that previously seen. PMID: 28777081
CUL3 interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells PMID: 27664236
we found that depletion of ATP citrate lyase suppressed tumor growth, which suggests that ATP citrate lyase-related inhibitors might be potential therapeutic approaches for breast cancer. PMID: 28443474
Results show that ACLY is a key phosphoprotein effector of IL-2-mediated T-cell responses. ACLY becomes phosphorylated on serine 455 in T lymphocytes upon IL-2-driven activation of AKT, and depletion or inactivation of ACLY compromises IL-2-promoted T-cell growth. PMID: 27067055
ACLY was also required for LMW-E-mediated transformation, migration, and invasion of breast cancer cells in vitro along with tumor growth in vivo In clinical specimens of breast cancer, the absence of LMW-E and low expression of adipophilin (PLIN2), a marker of lipid droplet formation, associated with favorable prognosis PMID: 26928812
ACL activity is associated with increased ATP. Activation of this IGF1/ACL/cardiolipin pathway combines anabolic signaling with induction of mechanisms needed to provide required ATP. PMID: 26039450
These results suggest that the combined expression of GLUT1 and ACLY could be a more valuable prognostic factor than their individual expression in node-negative patients with NSCLC. PMID: 25837797
Polymorphisms of ATP citrate lyase gene is associated with recurrence in colorectal cancer. PMID: 25890184
SNP rs9912300 in ACLY gene was significantly associated with response to therapy in hepatocellular carcinoma PMID: 25735330
The activation of AMPK under ACLY knockdown conditions may lead to p53 activation, ultimately leading to cellular senescence. PMID: 25367309
ATP citrate lyase mediates resistance of colorectal cancer cells to SN38. PMID: 24132143
These data indicate that inhibition of ACLY might affect both fatty acid elongation in ER and FAO in mitochondria, thereby explaining the TG accumulation with altered fatty acid composition. PMID: 24310723
ACLY inhibition exerts an anticancer effect via increased reactive oxygen species, and p-AMPK could be a predictive biomarker for its therapeutic outcome. PMID: 23506848
ATP citrate lyase functions in cancer stem cells to regulate stemness. PMID: 23807225
ATP citrate lyase is important for the pyruvate citrate shuttle and lipid synthesis in insulin secretion. PMID: 23225248
ACLY mRNA and protein levels markedly and quickly increase in activated macrophages. Importantly, ACLY activity inhibition as well as ACLY gene silencing lead to reduced nitric oxide, reactive oxygen species and prostaglandin E2 inflammatory mediators. PMID: 24051091
ACLY silencing clearly induces proliferation arrest and apoptosis in variety of cancer cell lines by affecting multiple downstream pathways. PMID: 22718913
The present review highlights current knowledge about the role of ACLY in cancer cells. PMID: 22787121
Chemical modification, steady-state and pre-steady-state kinetics, and rapid kinetics collectively demonstrate the essential role of the active site His760 in the ACL reaction: His760 acts as a phosphate acceptor to initiate the biosynthetic reaction. PMID: 22657152
Suggest that ATP citrate lyase may contribute to the pathogenesis of human epithelial ovarian cancer, and may serve as a novel therapeutic target. PMID: 22266777
crystals of ATP-citrate lyase diffracted to 2.3 A resolution PMID: 22102020
Differences between human and rodent pancreatic islets: low pyruvate carboxylase, atp citrate lyase, and pyruvate carboxylation and high glucose-stimulated acetoacetate in human pancreatic islets. PMID: 21454710
Data suggest that ATP-citrate lyase (ACLY) expression and activity can be suppressed by exogenous lipids and demonstrate a critical role for ACLY in pancreatic beta cell survival. PMID: 20693577
Data show that siRNA-mediated silencing of SREBP-1 and ATP citrate lyase significantly attenuated H(2)O(2)-induced senescence PMID: 20615871
Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography. PMID: 20558738
ACLY is a positive regulator of glycolysis in glioblastoma cells. PMID: 19795461
data presented indicate that the ATP citrate lyase pathway is operative in human platelets and may be responsible for increased acetyl-CoA in diabetic platelets which may be the cause of their excessive activity in the course of the disease PMID: 14681844
Atp citrate lyase is involved in lung cancer pathogenesis associated with metabolic abnormality and might offer a novel therapeutic target. PMID: 18922930
The activities of ATP citrate lyase were decreased by 57% in pancreatic islets of patients with type 2 diabetes. PMID: 19296078
findings suggest that ATP-citrate lyase activity is required to link growth factor-induced increases in nutrient metabolism to the regulation of histone acetylation and gene expression PMID: 19461003

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Subcellular Location

Cytoplasm, cytosol.

Protein Families

Succinate/malate CoA ligase beta subunit family; Succinate/malate CoA ligase alpha subunit family

Database Links

HGNC: 115

OMIM: 108728

KEGG: hsa:47

STRING: 9606.ENSP00000253792

UniGene: Hs.387567

Code	CSB-EP001158HU
Abbreviation	Recombinant Human ACLY protein, partial
MSDS	MSDS Datasheet
Size	US$306
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human ATP-citRate synthase (ACLY), partial

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