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anti-Human PDK3 Antibodies:
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Human Monoclonal PDK3 Primary Antibody for ELISA, WB - ABIN562161
Jeoung, Harris: Pyruvate dehydrogenase kinase-4 deficiency lowers blood glucose and improves glucose tolerance in diet-induced obese mice. in American journal of physiology. Endocrinology and metabolism 2008
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Human Polyclonal PDK3 Primary Antibody for ICC, IF - ABIN442546
Hou, Zhang, Han, Ge, Ma, Zhang, Moley, Schedl, Wang: Differing roles of pyruvate dehydrogenase kinases during mouse oocyte maturation. in Journal of cell science 2015
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Human Polyclonal PDK3 Primary Antibody for WB - ABIN391038
McFate, Mohyeldin, Lu, Thakar, Henriques, Halim, Wu, Schell, Tsang, Teahan, Zhou, Califano, Jeoung, Harris, Verma: Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells. in The Journal of biological chemistry 2008
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Human Polyclonal PDK3 Primary Antibody for FACS, WB - ABIN652286
Xu, Han, Epstein, Liu: Regulation of PDK mRNA by high fatty acid and glucose in pancreatic islets. in Biochemical and biophysical research communications 2006
Mouse (Murine) Polyclonal PDK3 Primary Antibody for IHC (p), WB - ABIN658195
Shimura, Nakai, Jiao, Osanai, Kashikura, Endo, Soga, Goda, Minamisawa: Metabolomic profiling analysis reveals chamber-dependent metabolite patterns in the mouse heart. in American journal of physiology. Heart and circulatory physiology 2013
The pyruvate dehydrogenase kinases (PDKs) PDK1 and PDK3 are direct targets of KDM4A and E2F1 and modulate the switch between glycolytic metabolism and mitochondrial oxidation.
We have identified a p.R158H PDK3 mutation in a Korean X-linked dominant Charcot-Marie-Tooth type 6 family
Accordingly, elevated levels of PDK1, PDK3, and PKM2 and reduced PK activity could be observed in iPSCs and human embryonic stem cells in the undifferentiated state
Reduced pyruvate flux due to R158H mutant PDK3-mediated hyper-phosphorylation of the pyruvate dehydrogenase complex is the underlying pathogenic cause of peripheral neuropathy in X-linked dominant Charcot-Marie-Tooth disease.
Findings suggest the HIF-1/PDK3 bioenergetic pathway as a new target for therapeutic intervention in metastatic melanoma.
mRNA levels not changed in skeletal muscle during fasting
analysis of residues in L2 and residues in the C-terminal region and the lipoyl-binding pocket of PDK3 which are critical determinants for the cross-talk between L2 and PDK3, which up-regulates PDK3 activity
crystal structure of the asymmetric PDHK3/lipoyl domain 2 complex; data suggest that the asymmetric complex represents a physiological state in which binding of a single L2-domain activates one of the PDHK protomers while inactivating another
PDK2, PDK3 and PDK4 are primary PPARbeta/delta target genes in humans underlining the importance of the receptor in the control of metabolism
Distinct structural mechanisms for inhibition of PDK3 by AZD7545, dichloroacetate, and radicol.
increased PDK3 expression due to elevated HIF-1alpha in cancer cells may play critical roles in metabolic switch during cancer progression and chemoresistance in cancer therapy
demonstrate that the increased PDK3 activity in patient fibroblasts (PDK3(R158H)) leads to the attenuation of PDC through hyper-phosphorylation of E1 at selected serine residues
These findings reveal that there are divergent roles of PDKs during oocyte maturation and indicate a new mechanism controlling meiotic structure.
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle, and thus is one of the major enzymes responsible for the regulation of glucose metabolism. The enzymatic activity of PDH is regulated by a phosphorylation/dephosphorylation cycle, and phosphorylation results in inactivation of PDH. The protein encoded by this gene is one of the three pyruvate dehydrogenase kinases that inhibits the PDH complex by phosphorylation of the E1 alpha subunit. This gene is predominantly expressed in the heart and skeletal muscles. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
pyruvate dehydrogenase kinase, isoenzyme 3
, pyruvate dehydrogenase, lipoamide, kinase isozyme 3, mitochondrial
, Pyruvate dehydrogenase kinase 3
, [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial
, pyruvate dehydrogenase kinase 3
, pyruvate dehydrogenase kinase, isozyme 3
, pyruvate dehydrogenase [lipoamide] kinase isozyme 3, mitochondrial-like
, pyruvate dehydrogenase kinase, isozyme 3b