ACLY Recombinant Monoclonal Antibody

Code CSB-RA712206A0HU
Size US$210
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  • Western Blot
    Positive WB detected in: L02 whole cell lysate, K562 whole cell lysate, Hela whole cell lysate, Raji whole cell lysate, A549 whole cell lysate
    All lanes: ACLY antibody at 1:1500
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 121, 120, 92 kDa
    Observed band size: 120 kDa
  • Immunofluorescence staining of HepG2 Cells with CSB-RA712206A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeated by 0.2% TritonX-100, and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4℃. Nuclear DNA was labeled in blue with DAPI. The secondary antibody was FITC-conjugated AffiniPure Goat Anti-Rabbit IgG (H+L).
  • Overlay histogram showing Hela cells stained with CSB-RA712206A0HU (red line) at 1:50. The cells were fixed with 70% Ethylalcohol (18h) and then incubated in 10% normal goat serum to block non-specific protein-protein interactions followedby the antibody (1µg/1*106 cells) for 1 h at 4℃.The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 30min at 4℃. Control antibody (green line) was Rabbit IgG (1µg/1*106 cells) used under the same conditions. Acquisition of >10,000 events was performed.
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Product Details

Uniprot No.
Target Names
ACLY
Alternative Names
ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (ACL) (Citrate cleavage enzyme), ACLY
Species Reactivity
Human
Immunogen
A synthesized peptide derived from human ATP citrate lyase
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Clonality
Monoclonal
Isotype
Rabbit IgG
Clone No.
3A5
Purification Method
Affinity-chromatography
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Form
Liquid
Tested Applications
ELISA, WB, IF, FC
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
IF 1:20-1:200
FC 1:20-1:200
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Description

The ACLY recombinant monoclonal antibody is generated using both protein and DNA recombinant technology. Firstly, a synthesized peptide derived from human ACLY was used to immunize mice, from which the spleen was extracted under aseptic conditions. The total RNA was extracted from spleen cells. The obtained cDNA synthesized by RNA reverse transcription served as the template for PCR amplification of the ACLY antibody gene. The ACLY antibody gene was then introduced into a vector, which was subsequently transfected into host cells for cultivation. Following cultivation, the ACLY recombinant monoclonal antibody was isolated and purified from the supernatant of the cell culture using affinity chromatography. It underwent rigorous verification and is suitable for detecting human ACLY protein in ELISA, WB, IF, and FC experiments.

The ATP citrate lyase (ACLY) protein is an enzyme that plays a key role in cellular metabolism, particularly in fatty acid synthesis. It is responsible for catalyzing the formation of acetyl-CoA from citrate, which is generated during the citric acid cycle within the mitochondria of cells. In addition to its role in lipid metabolism, ACLY has also been implicated in the regulation of gene expression and epigenetic modifications.

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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
  1. SLC25A1 and ACLY upregulation suggests that metabolic reprogramming in Behcet's syndrome involves the citrate pathway dysregulation. PMID: 30050389
  2. 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
  3. 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
  4. ACLY and ACSS2 are both activated to produce cytosolic Ac-CoA from glucose carbon for lipogenesis during human cytomegalovirus infection. PMID: 28167750
  5. 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
  6. 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
  7. CUL3 interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells PMID: 27664236
  8. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. Polymorphisms of ATP citrate lyase gene is associated with recurrence in colorectal cancer. PMID: 25890184
  14. SNP rs9912300 in ACLY gene was significantly associated with response to therapy in hepatocellular carcinoma PMID: 25735330
  15. The activation of AMPK under ACLY knockdown conditions may lead to p53 activation, ultimately leading to cellular senescence. PMID: 25367309
  16. ATP citrate lyase mediates resistance of colorectal cancer cells to SN38. PMID: 24132143
  17. 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
  18. 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
  19. ATP citrate lyase functions in cancer stem cells to regulate stemness. PMID: 23807225
  20. ATP citrate lyase is important for the pyruvate citrate shuttle and lipid synthesis in insulin secretion. PMID: 23225248
  21. 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
  22. ACLY silencing clearly induces proliferation arrest and apoptosis in variety of cancer cell lines by affecting multiple downstream pathways. PMID: 22718913
  23. The present review highlights current knowledge about the role of ACLY in cancer cells. PMID: 22787121
  24. 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
  25. 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
  26. crystals of ATP-citrate lyase diffracted to 2.3 A resolution PMID: 22102020
  27. 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
  28. 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
  29. Data show that siRNA-mediated silencing of SREBP-1 and ATP citrate lyase significantly attenuated H(2)O(2)-induced senescence PMID: 20615871
  30. Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography. PMID: 20558738
  31. ACLY is a positive regulator of glycolysis in glioblastoma cells. PMID: 19795461
  32. 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
  33. Atp citrate lyase is involved in lung cancer pathogenesis associated with metabolic abnormality and might offer a novel therapeutic target. PMID: 18922930
  34. The activities of ATP citrate lyase were decreased by 57% in pancreatic islets of patients with type 2 diabetes. PMID: 19296078
  35. 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

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