PDHA1 Mouse Monoclonal Antibody [Clone ID: 3H2-F8-B5]
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Recombinant protein of human pyruvate dehydrogenase (lipoamide) alpha 1 (PDHA1), nuclear gene encoding mitochondrial protein
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Specifications
Product Data | |
Clone Name | 3H2-F8-B5 |
Applications | IF, WB |
Recommended Dilution | WB: 1:1000, IF: 1:100 |
Reactivities | Human, Mouse |
Host | Mouse |
Isotype | IgG1 |
Clonality | Monoclonal |
Immunogen | The immunogen for PDHA1 antibody: purified recombinant human Pyruvate Dehydrogenase protein fragments expressed in E.coli. |
Formulation | Purified mouse monoclonal in buffer containing 0.1M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.02% sodium azide, 50%,glycerol |
Purification | Affinity purified |
Conjugation | Unconjugated |
Storage | Store at -20°C as received. |
Stability | Stable for 12 months from date of receipt. |
Predicted Protein Size | 43 kDa |
Gene Name | pyruvate dehydrogenase (lipoamide) alpha 1 |
Database Link | |
Background | 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), and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of two alpha and two beta subunits. This gene encodes the E1 alpha 1 subunit containing the E1 active site, and plays a key role in the function of the PDH complex. Mutations in this gene are associated with pyruvate dehydrogenase E1-alpha deficiency and X-linked Leigh syndrome. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. |
Synonyms | PDHA; PDHAD; PDHCE1A; PHE1A |
Reference Data | |
Protein Families | Druggable Genome |
Protein Pathways | Butanoate metabolism, Citrate cycle (TCA cycle), Glycolysis / Gluconeogenesis, Metabolic pathways, Pyruvate metabolism, Valine, leucine and isoleucine biosynthesis |
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