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Goat Anti-Pyruvate dehydrogenase / PDHX Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, E |
|---|---|
| Primary Accession | O00330 |
| Other Accession | NP_001159630, 8050, 27402 (mouse) |
| Reactivity | Human |
| Predicted | Mouse, Rat, Dog |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 54122 Da |
| Gene ID | 8050 |
|---|---|
| Other Names | Pyruvate dehydrogenase protein X component, mitochondrial, Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex, E3-binding protein, E3BP, Lipoyl-containing pyruvate dehydrogenase complex component X, proX, PDHX, PDX1 |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-Pyruvate dehydrogenase / PDHX Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PDHX |
|---|---|
| Synonyms | PDX1 |
| Function | Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. |
| Cellular Location | Mitochondrion matrix. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
The pyruvate dehydrogenase (PDH) complex is located in the mitochondrial matrix and catalyzes the conversion of pyruvate to acetyl coenzyme A. The PDH complex thereby links glycolysis to Krebs cycle. The PDH complex contains three catalytic subunits, E1, E2, and E3, two regulatory subunits, E1 kinase and E1 phosphatase, and a non-catalytic subunit, E3 binding protein (E3BP). This gene encodes the E3 binding protein subunit; also known as component X of the pyruvate dehydrogenase complex. This protein tethers E3 dimers to the E2 core of the PDH complex. Defects in this gene are a cause of pyruvate dehydrogenase deficiency which results in neurological dysfunction and lactic acidosis in infancy and early childhood. This protein is also a minor antigen for antimitochondrial antibodies. These autoantibodies are present in nearly 95% of patients with the autoimmune liver disease primary biliary cirrhosis (PBC). In PBC, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed. PBC eventually leads to cirrhosis and liver failure. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
References
Enzyme-assisted photosensitization with rose Bengal acetate induces structural and functional alteration of mitochondria in HeLa cells. Bottone MG, et al. Histochem Cell Biol, 2007 Mar. PMID 17024456.
Pyruvate dehydrogenase E3 binding protein (protein X) deficiency. Brown RM, et al. Dev Med Child Neurol, 2006 Sep. PMID 16904023.
A novel gross deletion caused by non-homologous recombination of the PDHX gene in a patient with pyruvate dehydrogenase deficiency. Min茅 M, et al. Mol Genet Metab, 2006 Sep-Oct. PMID 16843025.
PDC-E3BP is not a dominant T-cell autoantigen in primary biliary cirrhosis. McHugh A, et al. Liver Int, 2006 May. PMID 16629643.
Leigh's disease due to a new mutation in the PDHX gene. Schiff M, et al. Ann Neurol, 2006 Apr. PMID 16566017.
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