Pyruvate Dehydrogenase AntibodyProduct information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Metabolism
Pyruvate Dehydrogenase Antibody #2784
|2784S||100 µl (10 western blots)||---||In Stock||---|
|2784||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||43||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
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.
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).
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