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Phospho-ATP-Citrate Lyase (Ser455) (F4T8R) Rabbit mAb #97366

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  • WB
  • IP
  • IHC
  • F

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 125
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunohistochemistry (Paraffin) 1:400 - 1:1600
    Flow Cytometry (Fixed/Permeabilized) 1:400 - 1:1600

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-ATP-Citrate Lyase (Ser455) (F4T8R) Rabbit mAb recognizes endogenous levels of ATP-citrate lyase protein only when phosphorylated at Ser455 (equivalent to Ser454 in rat). Nonspecific plasma membrane staining was observed in a subset of tissues by immunohistochemistry.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser455 of human ATP-citrate lyase protein.

    Background

    ATP-citrate lyase (ACL) is a homotetramer that catalyzes the formation of acetyl-CoA and oxaloacetate (OAA) in the cytosol, which is the key step for the biosynthesis of fatty acids, cholesterol, and acetylcholine, as well as for gluconeogenesis (1). Nutrients and hormones regulate the expression level and phosphorylation of ATP-citrate lyase (1,2). It is phosphorylated by GSK-3 on Thr446 and Ser450 (3). Ser455 of ATP-citrate lyase has been reported to be phosphorylated by PKA and Akt (4,5). Phosphorylation on Ser455 abolishes the homotropic allosteric regulation by citrate and enhances the catalytic activity of the enzyme (2).

    ATP-citrate lyase is also critical in the pathogenesis of Parkinson’s disease (PD). α-synuclein mutations activate ATP-citrate lyase, leading to elevated cytoplasmic p300 activity. Hyperactivation of cytoplasmic p300 subsequently promotes mTORC1 signaling to inhibit autophagy, causing the aggregation of α-synuclein (6).
    For Research Use Only. Not for Use in Diagnostic Procedures.
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