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Phospho-Pyruvate Dehydrogenase α1 (Ser293) (E4V9L) Rabbit mAb (Biotinylated) #79790

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 43
    Source/Isotype Rabbit IgG
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Description

    This Cell Signaling Technology® antibody is the biotinylated version of the unconjugated Phospho-Pyruvate Dehydrogenase α1 (Ser293) (E4V9L) Rabbit mAb #37115 and is expected to exhibit the same species cross-reactivity. The concentration of the biotinylated antibody is 500 μg/mL. Peptide ELISA data were generated using the biotinylated antibody.
    MW (kDa) 43

    Product Usage Information

    Biotinylated antibodies are ideal for immunoassay technologies and high-throughput ELISA platforms that require antibody pairs where both antibodies are from the same host. Platforms utilizing biotinylated antibodies include, but are not limited to, MSD, xMAP, Quanterix Simoa, AlphaLISA, AlphaScreen, HTRF, LANCE, and TR-FRET.

    Optimal dilutions/working concentrations should be determined by the end user. Please contact us if you require the antibody clone biotinylated at a different concentration, a carrier-free formulation, or a more customized packaging solution.

    Storage

    Supplied in 140 mM NaCl, 3 mM KCl, 10 mM sodium phosphate (pH 7.4) dibasic, 2 mM potassium phosphate monobasic, 2 mg/mL BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Specificity / Sensitivity

    Phospho-Pyruvate Dehydrogenase α1 (Ser293) (E4V9L) Rabbit mAb (Biotinylated) recognizes endogenous levels of pyruvate dehydrogenase α1 protein only when phosphorylated at Ser293. Based on amino acid sequence comparisons, this antibody is predicted to detect endogenous levels of pyruvate dehydrogenase α2 protein only when phosphorylated at Ser291 residue.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser293 of human pyruvate dehydrogenase α1 protein.

    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 Ser293 to inactivate its activity (3,4). This phosphorylation contributes to the tumor metabolic reprogramming toward glycolysis in hypoxia by inhibiting the citric acid cycle (4).
    For Research Use Only. Not for Use in Diagnostic Procedures.
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