The PDK3 Polyclonal Antibody (PACO53534) is a valuable tool for researchers studying pyruvate dehydrogenase kinase 3 (PDK3), a key enzyme involved in the regulation of glucose metabolism. This antibody, produced in rabbits, exhibits high reactivity with human samples and is validated for use in Western blot applications. By binding to the PDK3 protein, this antibody allows for the detection and analysis of PDK3 levels in various cell types, making it an ideal choice for studies in metabolic disorders and cancer research.
PDK3 is known for its role in inhibiting the pyruvate dehydrogenase complex, thereby regulating the conversion of pyruvate to acetyl-CoA in the mitochondria. Dysregulation of PDK3 has been linked to metabolic diseases such as diabetes, as well as to the development and progression of cancer. Understanding the function of PDK3 is essential for unraveling the mechanisms underlying these diseases and for identifying potential therapeutic targets to intervene in their progression.
Western Blot. Positive WB detected in: Rat liver tissue. All lanes: Pdk3 antibody at 3µg/ml. Secondary. Goat polyclonal to rabbit IgG at 1/50000 dilution. Predicted band size: 48 kDa. Observed band size: 48 kDa.
Background:
Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species (By similarity).
PDHK3: an atypical protein kinase associated with the mitochondrial matrix. The PDHKs play crucial roles in switching metabolic flux from oxidative phosphorylation towards glycolysis. PDHK3 is present in testes, kidney, and brain. Contains a HATPase_c catalytic domain, found in several ATP-binding proteins including protein histidine kinases (PHKs), PHDKs, DNA gyrase B, topoisomerases, heat shock proteins, and DNA mismatch repair proteins. PDHK regulates glucose oxidation through inhibitory phosphorylation of the E1 alpha subunit of the mitochondrial pyruvate dehydrogenase complex (PDHC) at any one of 3 inhibitory serine residues. Inhibitory sites 1, 2, and 3 correspond to S293, S300, and S232 in human PDHA1, respectively. Four PDHK isoenzymes have been described, each with different site specificity: all four phosphorylate sites 1 and 2 but at different rates; for site 1 PDHK2 >PDHK4 >PDHK1 >PDHK3; for site 2, PDHK3> PDHK4 > PDHK2 > PDHK1. Only PDHK1 phosphorylates site 3. PDHKs are recruited to the PDHC by binding to a lipoyl group covalently attached to the inner lipoyl domain of the E2 component. PDHA1 deficiency is the most common enzyme defect in patients with primary lactic acidosis. Suppression of PDH by PDHK inhibits the conversion of pyruvate to acetyl-CoA, attenuates mitochondrial respiration, and may contribute to the increased lactate production observed in many tumors. The PDH pathway is repressed in a majority of non-small cell lung carcinomas. Inhibited by AZD7545, dichloroacetate (DCA), and radicicol. Radicicol inhibits kinase activity by binding directly to the ATP-binding pocket of PDHK, similar to HSP90 from the same ATPase/kinase superfamily.Protein type: Kinase, protein; Protein kinase, atypical; Mitochondrial; EC 2.7.11.2; ATYPICAL group; PDHK familyCellular Component: mitochondrionMolecular Function: ATP binding; protein kinase activity; protein serine/threonine kinase activity; pyruvate dehydrogenase (acetyl-transferring) kinase activityBiological Process: peptidyl-serine phosphorylation; regulation of acetyl-CoA biosynthetic process from pyruvate