|Application ||WB, IHC, FC, ICC, E|
|Reactivity||Human, Rat, Monkey|
|Description||Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. (provided by RefSeq). Tissue specificity: Expressed predominantly in the heart.|
|Immunogen||Purified recombinant fragment of human PDK1 expressed in E. Coli.|
|Formulation||Ascitic fluid containing 0.03% sodium azide. |
|Other Names||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial, 126.96.36.199, Pyruvate dehydrogenase kinase isoform 1, PDH kinase 1, PDK1, PDHK1|
|Dilution||WB~~1/500 - 1/2000|
IHC~~1/200 - 1/1000
IF~~1/200 - 1/1000
FC~~1/200 - 1/400
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PDK1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.|
|Cellular Location||Mitochondrion matrix|
|Tissue Location||Expressed predominantly in the heart. Detected at lower levels in liver, skeletal muscle and pancreas|
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