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Key Documents

AV48136

Sigma-Aldrich

Anti-PDHA1 (AB1) antibody produced in rabbit

IgG fraction of antiserum

Synonyme(s) :

Anti-PDHA, Anti-PDHCE1A, Anti-PHE1A, Anti-Pyruvate dehydrogenase (lipoamide) α 1

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

40 kDa

Espèces réactives

human, mouse, guinea pig, rabbit, dog, rat

Concentration

0.5 mg - 1 mg/mL

Technique(s)

western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... PDHA1(5160)

Description générale

PDHA1 codes for the α1 subunit of the pyruvate dehydrogenase complex and modulates the activity of the complex. PDHA1 mutations have been implicated in pyruvate dehydrogenase deficiency.
Rabbit Anti-PDHA1 antibody recognizes bovine, chicken, pig, human, mouse, rat, and canine PDHA1.

Immunogène

Synthetic peptide directed towards the N terminal region of human PDHA1

Application

Rabbit Anti-PDHA1 antibody is suitable for western blot applications at a concentration of 5μg/ml.

Actions biochimiques/physiologiques

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. The PDH complex is composed of multiple copies of 3 enzymes: E1 (PDHA1); dihydrolipoyl transacetylase (DLAT); and dihydrolipoyl dehydrogenase (DLD). The E1 enzyme is a heterotetramer of 2 alpha and 2 beta subunits. The E1-alpha subunit contains the E1 active site and plays a key role in the function of the PDH complex.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. The PDH complex is composed of multiple copies of 3 enzymes: E1 (PDHA1); dihydrolipoyl transacetylase (DLAT; MIM 608770) (E2; EC 2.3.1.12); and dihydrolipoyl dehydrogenase (DLD; MIM 238331) (E3; EC 1.8.1.4). The E1 enzyme is a heterotetramer of 2 alpha and 2 beta subunits. The E1-alpha subunit contains the E1 active site and plays a key role in the function of the PDH complex (Brown et al., 1994 [PubMed 7853374]).[supplied by OMIM]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Séquence

Synthetic peptide located within the following region: MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGP

Forme physique

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

E Ostergaard et al.
Journal of inherited metabolic disease, 32 Suppl 1, S235-S239 (2009-06-12)
The pyruvate dehydrogenase (PDH) complex is a mitochondrial multienzyme that catalyses the irreversible oxidative decarboxylation of pyruvate to acetyl-CoA. We report four novel PDHA1 mutations in patients with pyruvate dehydrogenase deficiency. Analysis of PDH activity showed decreased activity in fibroblasts

Articles

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