Recombinant Human ATP citrate lyase / ATPCL Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0287

Recombinant Human ATP citrate lyase / ATPCL Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0287
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Product Overview

Tag His
Host Species Human
Accession P53396
Background ATP citrate lyase, also known as Acly or Acl, is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is composed of two polymer chains which are polypeptides in human. ATP citrate lyase is responsible for catalyzing the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, along with the hydrolysis of ATP. A definitive role for ATP citrate lyase in tumorigenesis has emerged from ATP citrate lyase RNAi and chemical inhibitor studies, showing that ATP citrate lyase inhibition limits tumor cell proliferation and survival and induces differentiation in vitro. In vivo, it reduces tumor growth leading to a cytostatic effect and induces differentiation.
Description A DNA sequence encoding the human ACLY (P53396) (Met 1-Met 1101) was expressed, with a His tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Met 1-Met 1101
Molecular Weight The recombinant human ACLY consists of 1120 a.a. and has a calculated molecular mass of 123 kDa. It migrates as an approximately 110 kDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 8.0, 10% gly.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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.
Subcellular Location Cytoplasm, cytosol.
Protein Families Succinate/malate CoA ligase beta subunit family; Succinate/malate CoA ligase alpha subunit family
Database References

Gene Functions References

  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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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