antibody

PDK1 Antibody

MBS850452

0.1 mg

290 USD

monoclonal

mouse

nonconjugated

4A11

human, rat

western blot, ELISA, immunohistochemistry, immunocytochemistry, flow cytometry, enzyme immunoassay

Antibody

PDK1 Antibody

PDK1

PDK1

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial isoform 2; [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial; [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial; [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial; PDH kinase 1; pyruvate dehydrogenase kinase, isoenzyme 1; mitochondrial pyruvate dehydrogenase, lipoamide, kinase isoenzyme 1; pyruvate dehydrogenase kinase, isozyme 1; Pyruvate dehydrogenase kinase isoform 1; PDH kinase 1

PDK1

PDK1; PDK1; PDHK1; PDH kinase 1

PDK1_HUMAN

Monoclonal

4A11

Mouse

Human, Monkey, Rat

436

Ascitic fluid containing 0.03% sodium azide.

100ug/100ul

Store at 4 degree C, for long term storage, store at -20 degree C.

Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), ELISA (EIA), Flow Cytometry (FC)

WB: 1/500 - 1/2000, IHC:1/200-1/1000, IF: 1/200-1/1000, FC:1/200-1/400, ELISA: Propose dilution 1/10000. Not yet tested in other applications.

Immunogen: Purified recombinant fragment of human PDK1 expressed in E. Coli. Species: Mouse IgG1

Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells; Autophagy antibody

Background: 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.

4505689

NP_002601.1

NM_002610.4

44kDa

DNA Damage Response (only ATM Dependent) Pathway (198827); EPO Receptor Signaling Pathway (198882); ErbB Signaling Pathway (198844); HIF-1 Signaling Pathway (695200); Integrated Pancreatic Cancer Pathway (711360); Metabolism Pathway (477135); Pyruvate Metabolism Pathway (106205); Pyruvate Metabolism And Citric Acid (TCA) Cycle Pathway (106327); Regulation Of Pyruvate Dehydrogenase (PDH) Complex Pathway (106109); The Citric Acid (TCA) Cycle And Respiratory Electron Transport Pathway (477137)

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. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jun 2013]

PDHK1: an ubiquitously expressed, atypical protein kinase associated with the mitochondrial matrix. The PDHKs play crucial roles in switching metabolic flux from oxidative phosphorylation towards glycolysis. PDHK1 is detected in heart, pancreatic islets, and skeletal muscles. 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 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. PDHK1 is a direct HIF-1 target gene. 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; Mitochondrial; EC 2.7.11.2; Protein kinase, atypical; ATYPICAL group; PDHK family. Chromosomal Location of Human Ortholog: 2q31.1. Cellular Component: mitochondrion; mitochondrial matrix; mitochondrial pyruvate dehydrogenase complex. Molecular Function: protein binding; pyruvate dehydrogenase (acetyl-transferring) kinase activity; ATP binding; protein kinase activity. Biological Process: cellular metabolic process; cell proliferation; glucose metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate; pyruvate metabolic process; induction of apoptosis by oxidative stress; protein amino acid phosphorylation

0.1 mg

290 USD