The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial matrix enzyme complex that functions as the primary link between glycolysis and the tricarboxylic acid (TCA) cycle by catalyzing the irreversible conversion of pyruvate into acetyl-CoA. The E1 enzyme of the PDH complex is made up of a heterotetramer of two å and two ∫ subunits. The E1-å subunit (PDH-E1å) contains the E1 active site and plays a key role in the function of the PDH complex. The PDH complex is regulated by phosphorylation and dephosphorylation of PDH-E1å. The gene encoding for PDH-E1å maps to chromosome Xp22-q24, and a 20-bp deletion in the last exon of this gene is sufficient to cause PDH deficiency, which causes a broad range of symptoms including the development of seizures, mental retardation and spasticity, as well as intermittent episodes of lactic acidosis associated with cerebellar ataxia.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of PDH-E1&alpha of mouse rat and human origin by WB IP and ELISA
Tissue Specificity
recommended for detection of PDH-E1α of mouse, rat and human origin by WB, IP and ELISA