The core of PDC is composed of sixty dihydrolypoyl acetyltransferase (E2) subunits that bind directly to PDK2 and enhance PDK2 kinase activity. Upregulation of PDK isoenzymes occurs during starvation conditions, rerouting acetyl-CoA generation by facilitating fatty acid oxidation. PDKs contain five conserved regions and are mechanistically similar to bacterial His-kinases, in that both require histidine residues for activity. In mammals, transcripts for PDK2 are ubiquitously expressed with high levels in heart and skeletal muscle and decreased levels in spleen and lung.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
