Render Target: STATIC
Render Timestamp: 2024-10-11T10:06:06.287Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-04-19 20:01:09.365
Product last modified at: 2024-07-16T16:45:08.376Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Pyruvate Dehydrogenase α1 (Ser232) Antibody #15289

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 43
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

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

    Protocol

    Specificity / Sensitivity

    Phospho-Pyruvate Dehydrogenase α1 (Ser232) Antibody recognizes endogenous levels of pyruvate dehydrogenase α1 protein only when phosphorylated at Ser232.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser232 of human pyruvate dehydrogenase α1 protein. Antibodies are purified by peptide affinity chromatography.

    Background

    The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. The reaction of oxidative decarboxylation of pyruvate serves as a critical link between glycolysis and the citric acid cycle. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is composed of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration, and early death (2).

    Pyruvate dehydrogenase kinase 1 phosphorylates pyruvate dehydrogenase (E1) α1 subunit at Ser232 and Ser300, which is important for ubiquitin-dependent degradation of this subunit (3).
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