Cell Signaling Technology

Product Pathways - Metabolism

Pyruvate Dehydrogenase Antibody #2784

Applications Reactivity Sensitivity MW (kDa) Source
W IF-IC H M R Mk Endogenous 43 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Pyruvate Dehydrogenase Antibody detects endogenous levels of total α1 and α2 subunits of pyruvate dehydrogenase protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequences of both α1 and α2 subunits of human pyruvate dehydrogenase. Antibodies are purified by peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using Pyruvate Dehydrogenase Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of HeLa cells using Pyruvate Dehydrogenase Antibody (green) showing colocalization with mitochondria that have been labeled with MitoTracker® Red CMXRos (red). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

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. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised 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).

  1. Strumiło, S. (2005) Acta Biochim Pol 52, 759-64.
  2. Stacpoole, P.W. et al. (2003) Curr Gene Ther 3, 239-45.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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