

| Numéro de catalogue | HY552014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Description |
Anti-PDHA1 Polyclonal Antibody (HY552014) is a rabbit polyclonal antibody detecting PDHA1 in ELISA, IHC, WB. Suitable for Human, Mouse, Rat, Bovine, and Macaca fascicularis.
Highlights
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| Reactivité des espèces | Human, Mouse, Rat | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Espèce hôte | Rabbit | ||||||||
| Clonalité | Polyclonal | ||||||||
| Isotype | IgG | ||||||||
| Immunogène | E. coli - derived recombinant Human PDHA1 (Phe30-Ser390). | ||||||||
| Cible | PHE1A, PDHE1-A type I, Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial, PDHA1 | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Numéro d'accès | P08559 | ||||||||
| Forme | Liquid | ||||||||
| Tampon de stockage | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Reférez-vous aux informations spécifiques sur le tampon dans la copie papier du datasheet ou dans le COA spécifique au lot. |
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| Informations d'utilisation du produit |
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| Stabilité et stockage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Contexte | Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (PDHA1) is a ~43 kDa protein. Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex. The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2. 1. Seifert, F. et al. (2007) Biochemistry 46, 6277-87. PMID: 17474719 2. Kato, M. et al. (2008) Structure (London, England : 1993) 16, 1849-59. PMID: 19081061 3. Korotchkina, LG. et al. (1995) The Journal of biological chemistry 270, 14297-304. PMID: 7782287 | ||||||||
| Note | For research use only. |
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