Pyruvate Dehydrogenase Kinase Isozyme 2 (PDK2) Recombinant Protein | PDK2 recombinant protein

Recombinant Pyruvate Dehydrogenase Kinase Isozyme 2 (PDK2)

Cat. Num. AAA2010407

• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Pyruvate Dehydrogenase Kinase Isozyme 2 (PDK2); Recombinant Pyruvate Dehydrogenase Kinase Isozyme 2 (PDK2); PDK2 recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with two N-terminal Tags, His-tag and T7-tag, its sequence is listed below.; MGSSHHHHHH SSGLVPRGSH MASMTGGQQM GRGSEF-LDRFYL SRISIRMLIN QHTLIFDGST NPAHPKHIGS IDPNCSVSDV VKDAYDMAKL LCDKYYMASP DLEIQEVNAT NANQPIHMVY VPSHLYHMLF ELFKNAMRAT VESHESSLTL PPIKIMVALG EEDLSIKMSD RGGGVPLRKI ERLFSYMYST APTPQPGTGG TPLAGFGYGL PISRLYAKYF QGDLQLFSME GFGTDAVIYL KALSTDSVER LPVYNKSAW
• Sequence Length: 407

• Applicable Applications for PDK2 recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Mus musculus (Mouse)
• Expression System: Prokaryotic expression
• Residues: Leu155~Trp379 (Accession # Q9JK42) with two N-terminal Tags, His-tag and T7-tag
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-Page

NCBI and Uniprot Product Information

• NCBI GI #: 226958643
• NCBI GeneID: 18604
• NCBI Accession #: NP_598428.2
• NCBI GenBank Nucleotide #: NM_133667.2
• UniProt Accession #: Q9JK42; Q8VC63
• Molecular Weight: 29.0kDa
• NCBI Official Full Name: pyruvate dehydrogenase kinase, isoenzyme 2
• NCBI Official Synonym Full Names: pyruvate dehydrogenase kinase, isoenzyme 2
• NCBI Official Symbol: Pdk2
• NCBI Protein Information: pyruvate dehydrogenase kinase, isoenzyme 2; PDH kinase 2; pyruvate dehydrogenase 2; pyruvate dehydrogenase kinase, isozyme 2; [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial; [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial
• UniProt Protein Name: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial
• UniProt Gene Name: Pdk2
• UniProt Synonym Gene Names: PDH kinase 2
• UniProt Entry Name: PDK2_MOUSE

Uniprot Description

PDHK2: an atypical protein kinase associated with the mitochondrial matrix. The PDHKs play crucial roles in switching metabolic flux from oxidative phosphorylation towards glycolysis. PDHK2 is expressed in all tissues. 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: Mitochondrial; Kinase, protein; EC 2.7.11.2; Protein kinase, atypical; ATYPICAL group; PDHK family; PDHK subfamily

Cellular Component: nucleoplasm; mitochondrion; cytoplasm; pyruvate dehydrogenase complex; mitochondrial pyruvate dehydrogenase complex

Molecular Function: transferase activity; protein serine/threonine kinase activity; protein binding; protein homodimerization activity; protein heterodimerization activity; protein complex binding; nucleotide binding; kinase activity; pyruvate dehydrogenase (acetyl-transferring) kinase activity; ATP binding

Biological Process: peptidyl-serine phosphorylation; carbohydrate metabolic process; insulin receptor signaling pathway; regulation of pH; glucose metabolic process; cellular response to nutrient; regulation of gluconeogenesis; regulation of acetyl-CoA biosynthetic process from pyruvate; glucose homeostasis; protein amino acid phosphorylation; phosphorylation