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Validated All-in-One™ qPCR Primer for PDHA1(NM_000284.3) Search again
Product ID:
HQP012901
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
E1alpha, PDHA, PDHAD, PDHCE1A, PHE1A
Gene Description:
pyruvate dehydrogenase E1 subunit alpha 1
Target Gene Accession:
NM_000284.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The pyruvate dehydrogenase complex is a nuclear-encoded mitochondrial matrix multienzyme complex that provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle by catalyzing the irreversible conversion of pyruvate into acetyl-CoA.
Gene References into function
- model of the pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and binding of the E1 and E3 components
- determinant spreading might underlie the autoimmunity against Elalpha.
- PDHA1 gene mutations may have a role in Pyruvate dehydrogenase E1 subunit deficiency
- Molecular genetic analysis of the X-chromosomal E1alpha subunit of PDH showed three new mutations in phylogenetically conserved areas of the protein: Glu358Lys in patient 1; Arg88Lys in patient 2 and 3 (brothers); and Leu216Ser in patient 4.
- Short-term elevation in plasma non-esterified fatty acids at rest increases PDH-E1alpha phosphorylation, but exercise overrules this effect and phosphorylation leads to even dephosphorylation during exercise with intralipid infusion.
- Attenuated PDHa activity contributes to the preferential oxidation of n-6 PUFA during moderate-intensity exercise.
- Resting PDH protein content and phosphorylation on PDH-E1 alpha sites 1 and 2 were higher in vastus lateralis than in triceps and deltoid as was the activity of oxidative enzymes
- two synonymous mutations expand the spectrum of rare PDHA1 splicing mutations, all of which are located in non canonical splice sites.
