recommended for detection of PDK4 of human origin by WB, IP, IF, IHC(P) and ELISA
Modification Notes
Pyruvate dehydrogenase kinase family members (PDK1, 2, 3, 4) are serine kinases that catalyze phosphorylation of the E1å subunit of the pyruvate dehydrogenase complex (PDC). PDC activity is controlled through phosphorylation and dephosphorylation of the E1å subunit, which leads to inactivation and reactivation, respectively. Upregulation of PDK isoenzymes occurs during starvation conditions, where acetyl-CoA is alternatively generated through fatty acid oxidation. PDKs contain five conserved regions and are mechanistically similar to bacterial His-kinases since both require histidine residues for activity. In mammals, transcripts for PDK4 are most abundant in heart and skeletal muscle. PDK4 protein levels increase in starved or diabetic rat cardiac muscle and decrease upon re-feeding or insulin exposure, suggesting that PDK4 protein levels are important for long-term regulation of PDC activity in heart.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
WB:1:500~1:2000 IP:1:100~1:500 IF:1:200~1:500 IHC:1:50~1:200 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of PDK4 of human origin by WB IP IF IHC(P) and ELISA
Tissue Specificity
recommended for detection of PDK4 of human origin by WB, IP, IF, IHC(P) and ELISA