Metabolism
Antibodies
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 | | Anti-phospho-PDHE1-A type I (Ser293)
In many organisms, the pyruvate dehydrogenase (PDH) complex catalyzes the overall, irreversible conversion of pyruvate to acetyl-CoA and CO2 in the aerobic pathway. This complex also serves as a key regulator for cardiac substrate selection. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1 or PDHE1-A type I), dihydrolipoamide acetyltransferase (E2), and lipoamide dehydrogenase (E3). PDH is regulated by both pyruvate dehydrogenase kinase (PDK)-mediated phosphorylation and feedback inhibition. This image showes confocal fluorescent analysis of DCA-treated HEK293 cells using Anti-phospho-PDHE1-A type I (Ser293) (Red). Nuclei are stained with DAPI (Blue). This antibody positively stains the cytoplasm.
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 | | MILLIPLEX MAP Multi-species Pyruvate Dehydrogenase (PDH) Complex Magnetic Bead Panel, PDHMAG-13K
The Pyruvate Dehydrogenase Complex (PDH Complex or PDC) is a key regulator of cellular energy metabolism, and has roles in numerous diseases including cancer, neurodegeneration, cardiovascular disease, and diabetes. PDH catalyzes the irreversible conversion of pyruvate to acetyl-CoA. PDH Complex activity is regulated by PDKs (PDH kinases) and PDPs (PDH phosphatases). One of the modes of action for dichloroacetate (DCA), a potential treatment for cancer and lactic acidosis, is to inhibit PDK activity resulting in decreased PDH Complex phosphorylation and therefore increased PDH activity.
This bar graph illustrates PDH complex phosphorylation changes in HepG2 cells treated with DCA.
» Learn More
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Metabolism
Antibodies
Anti-phospho-PDHE1-A type I (Ser293)
In many organisms, the pyruvate dehydrogenase (PDH) complex catalyzes the overall, irreversible conversion of pyruvate to acetyl-CoA and CO2 in the aerobic pathway. This complex also serves as a key regulator for cardiac substrate selection. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1 or PDHE1-A type I), dihydrolipoamide acetyltransferase (E2), and lipoamide dehydrogenase (E3). PDH is regulated by both pyruvate dehydrogenase kinase (PDK)-mediated phosphorylation and feedback inhibition. This image showes confocal fluorescent analysis of DCA-treated HEK293 cells using Anti-phospho-PDHE1-A type I (Ser293) (Red). Nuclei are stained with DAPI (Blue). This antibody positively stains the cytoplasm.
MILLIPLEX MAP Multi-species Pyruvate Dehydrogenase (PDH) Complex Magnetic Bead Panel, PDHMAG-13K
The Pyruvate Dehydrogenase Complex (PDH Complex or PDC) is a key regulator of cellular energy metabolism, and has roles in numerous diseases including cancer, neurodegeneration, cardiovascular disease, and diabetes. PDH catalyzes the irreversible conversion of pyruvate to acetyl-CoA. PDH Complex activity is regulated by PDKs (PDH kinases) and PDPs (PDH phosphatases). One of the modes of action for dichloroacetate (DCA), a potential treatment for cancer and lactic acidosis, is to inhibit PDK activity resulting in decreased PDH Complex phosphorylation and therefore increased PDH activity.
This bar graph illustrates PDH complex phosphorylation changes in HepG2 cells treated with DCA.
