Anti-ATP citrate lyase (phospho T447 + S451) antibody [EP737Y] (ab53007)


  • Product nameAnti-ATP citrate lyase (phospho T447 + S451) antibody [EP737Y]
    See all ATP citrate lyase primary antibodies
  • Description
    Rabbit monoclonal [EP737Y] to ATP citrate lyase (phospho T447 + S451)
  • Specificityab53007 only detects ATP-citrate lyase phosphorylated on Threonine 447 and Serine 451.
  • Tested applicationsSuitable for: WB, ICC/IF, IPmore details
    Unsuitable for: Flow Cyt or IHC-P
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    A synthetic phospho-peptide corresponding to residues surrounding Thr447 and Ser451 of human ATP-citrate (pro-S) lyase.

  • Positive control
    • 3T3 cytoplasmic cell lysate HeLa cells
  • General notes

    This product is a recombinant rabbit monoclonal antibody.


    Produced using Abcam’s RabMAb® technology. RabMAb® technology is covered by the following U.S. Patents, No. 5,675,063 and/or 7,429,487.


Associated products


Our Abpromise guarantee covers the use of ab53007 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/1000. Detects a band of approximately 100 kDa (predicted molecular weight: 122 kDa).
ICC/IF 1/100 - 1/250.
IP 1/10 - 1/100.
  • Application notesIs unsuitable for Flow Cyt or IHC-P.
  • Target

    • FunctionATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.
    • Sequence similaritiesIn 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.
      Contains 1 ATP-grasp domain.
    • Post-translational
      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.
    • Cellular localizationCytoplasm.
    • Information by UniProt
    • Database links
    • Alternative names
      • ACL antibody
      • Acly antibody
      • ACLY_HUMAN antibody
      • ATP citrate (pro-S) lyase antibody
      • ATP citrate lyase antibody
      • ATP citrate synthase antibody
      • ATP-citrate (pro-S-)-lyase antibody
      • ATP-citrate synthase antibody
      • ATPcitrate synthase antibody
      • ATPCL antibody
      • Citrate cleavage enzyme antibody
      • CLATP antibody
      • OTTHUMP00000164773 antibody
      see all

    Anti-ATP citrate lyase (phospho T447 + S451) antibody [EP737Y] images

    • All lanes : Anti-ATP citrate lyase (phospho T447 + S451) antibody [EP737Y] (ab53007) at 1/1000 dilution

      Lane 1 : (A) 3T3 cell lysate (untreated cells)
      Lane 2 : (B) 3T3 cell lysate (insulin treated cells)

      Lysates/proteins at 10 µg per lane.

      goat anti-rabbit HRP labelled at 1/2000 dilution

      Predicted band size : 122 kDa
      Observed band size : 100 kDa (why is the actual band size different from the predicted?)
    • ab53007 stained HeLa cells at 1/100-1/250 dilution.

    References for Anti-ATP citrate lyase (phospho T447 + S451) antibody [EP737Y] (ab53007)

    This product has been referenced in:
    • Grunert T  et al. A comparative proteome analysis links tyrosine kinase 2 (Tyk2) to the regulation of cellular glucose and lipid metabolism in response to poly(I:C). J Proteomics 74:2866-80 (2011). WB . Read more (PubMed: 21787891) »
    • Chu KY  et al. ATP-citrate lyase reduction mediates palmitate-induced apoptosis in pancreatic beta cells. J Biol Chem 285:32606-15 (2010). Read more (PubMed: 20693577) »

    See all 2 Publications for this product

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