Anti-PDK2

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Pyruvate dehydrogenase kinase isoenzyme 2, is an enzyme that in humans is encoded by the PDK2 gene. To find human PDKs, Gudi et al.(1995) used oligonucleotide primers to screen a human liver cDNA library by PCR. The human PDK2 gene encodes a protein with a predicted molecular mass of 46,181 Da that shares 96% identity with that of the rat gene. Northern blot analysis showed that the PDK2 message was found in many tissues, with the highest level in heart and skeletal muscle, intermediate levels in brain, kidney, pancreas and liver, and low levels in placenta and lung. Protein function: Kinase that plays a key role in the 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. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis. [The UniProt Consortium]