Rabbit PDHA1 Polyclonal Antibody | anti-PDHA1 antibody

PDHA1 Antibody

Cat. Num. AAA2516684

• Gene Names: PDHA1; PDHA; PDHAD; PHE1A; PDHCE1A
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry, Immunofluorescence
• Purity: Antigen affinity purification
• Synonyms: PDHA1; Polyclonal Antibody; PDHA1 Antibody; PDHA; PDHCE1A; PHE1A; anti-PDHA1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Antigen affinity purification
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 359

• Applicable Applications for anti-PDHA1 antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)
• Immunogen: Recombinant protein of human PDHA1
• Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3
• Santa Cruz Alternative: Potential replacement for Santa Cruz Biotechnology antibody catalog# sc-133898 / sc-292543
• Preparation and Storage: Store at -20 degree C (regular) and -80 degree C (long term). Avoid freeze / thaw cycles.

Western Blot (WB)

(Western blot analysis of extracts of various cell lines, using PDHA1 antibody.)

Immunohistochemistry (IHC)

(Immunohistochemistry of paraffin-embedded human kidney using PDHA1 antibody at dilution of 1:200 (x400 lens))

Immunohistochemistry (IHC)

(Immunohistochemistry of paraffin-embedded mouse kidney using PDHA1 antibody at dilution of 1:200 (x400 lens))

Immunofluorescence (IF)

(Immunofluorescence analysis of U2OS cell using PDHA1 antibody. Blue: DAPI for nuclear staining.)

Related Product Information for anti-PDHA1 antibody

The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: alpha and beta. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the alpha subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration and early death (2).

NCBI and Uniprot Product Information

• NCBI GI #: 291084757
• NCBI GeneID: 5160
• NCBI Accession #: NP_001166927.1
• NCBI GenBank Nucleotide #: NM_001173456.1
• Molecular Weight: 47,580 Da
• NCBI Official Full Name: pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial isoform 4
• NCBI Official Synonym Full Names: pyruvate dehydrogenase (lipoamide) alpha 1
• NCBI Official Symbol: PDHA1
• NCBI Official Synonym Symbols: PDHA; PDHAD; PHE1A; PDHCE1A
• NCBI Protein Information: pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; pyruvate dehydrogenase complex, E1-alpha polypeptide 1
• UniProt Protein Name: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
• Protein Family: Pyruvate dehydrogenase E1 component
• UniProt Gene Name: PDHA1
• UniProt Synonym Gene Names: PHE1A
• UniProt Entry Name: ODPA_HUMAN

NCBI Description

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.[provided by RefSeq, Mar 2010]

Uniprot Description

PDHA1: a mitochondrial matrix enzyme that catalyzes the oxidative decarboxylation of pyruvate, producing acetyl-CoA and CO2. A key enzyme in controlling the balance between lipid and glucose oxidation depending on substrate availability. The pyruvate dehydrogenase (PDH) holoenzyme is a multi-enzyme complex (PDHC) that contains 20-30 copies of pyruvate decarboxylase tetramers (2 alpha:2 beta)(E1), 60 copies of dihydrolipoamide acetyltransferase (E2), six homodimers of dihydrolipoamide dehydrogenase (E3), plus E3 binding proteins. The activity of PDH is tightly regulated by phosphorylation. The phosphorylation of at least one of three specific serine residues in E1 subunit by PDHK inactivates the PDHC, while dephosphorylation by PDP restores its activity. Sites 1, 2, and 3 of PDHA1 are S293, S300, and S232, respectively. Four PDHK isoenzymes have been described, each with different site specificity: all four phosphorylate sites 1 and 2 but at different rates; for site 1 PDHK2 >PDHK4 >PDHK1 >PDHK3; for site 2, PDHK3> PDHK4 > PDHK2 > PDHK1. Only PDHK1 phosphorylates site 3. PDHA1 deficiency is the most common enzyme defect in patients with primary lactic acidosis.

Protein type: Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - butanoate; Mitochondrial; EC 1.2.4.1; Carbohydrate Metabolism - citrate (TCA) cycle; Amino Acid Metabolism - valine, leucine and isoleucine biosynthesis; Carbohydrate Metabolism - pyruvate; Oxidoreductase

Chromosomal Location of Human Ortholog: Xp22.1

Cellular Component: mitochondrion; mitochondrial matrix; pyruvate dehydrogenase complex; nucleus

Molecular Function: pyruvate dehydrogenase activity; pyruvate dehydrogenase (acetyl-transferring) activity

Biological Process: acetyl-CoA biosynthetic process from pyruvate; cellular metabolic process; glycolysis; tricarboxylic acid cycle; glucose metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate; pyruvate metabolic process

Disease: Pyruvate Dehydrogenase E1-alpha Deficiency