Anti-phospho-PDHE1-A type I (Ser293) Antibody

Control
Untreated and DCA-treated HEK293 cell lysates

Evaluated by Western Blotting in untreated and Dichloroacetate (DCA) treated HEK-293T cells.

Western Blotting Analysis (WB): A 1:1,000 dilution from a representative lot detected PDHE1-A type I phosphorylated at serine 293 in lysate from untreated HEK-293T cells.

Detect phospho-PDHE1-A type I (Ser293) using this Anti-phospho-PDHE1-A type I (Ser293) Antibody validated for use in WB, IC & IP.

Research Category
Metabolism

Research Sub Category
Glucose/Glycogen Metabolism

Tested Applications

Peptide Inhibition Assay: Target band detection in lysate from HEK-293T cells was prevented by pre-blocking of a representative lot with the immunogen phosphorylated peptide, but not the corresponding non-phosphorylated peptide.

Immunocytochemistry Analysis: A 1:1,000 dilution from a representative lot detected PDH-E1a phosphorylated at serine 293 in untreated HEK293 cells.

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

This antibody recognizes PDHE1-A type I phosphorylated at Ser293.

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.

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (also known as PDHE1-A type I, UniProt: P08559) is encoded by the PDHA1 (also known as PHE1A) gene (Gene ID: 5160) in human. In many organisms, the pyruvate dehydrogenase (PDH) complex catalyzes the overall, irreversible conversion of pyruvate to acetyl-CoA and CO2 in the aerobic pathway. This complex also serves as a key regulator for cardiac substrate selection. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1 or PDHE1-A type I), dihydrolipoamide acetyltransferase (E2), and lipoamide dehydrogenase (E3). PDHE1-A is ubiquitously expressed and is found abundantly in heart muscle, skeletal muscle and tongue. This enzyme is predominantly localized in the mitochondrion matrix, where it functions in energy production. However, recent studies have shown that PDHE1-A can also localize to the cytosol, where it interacts with various proteins, including IKKβ, influencing pathways such as NF- B signaling. Four isoforms of PDHE1-A type I have been described that are produced by alternative splicing. PDH is regulated by both pyruvate dehydrogenase kinase (PDK)-mediated phosphorylation and feedback inhibition. Phosphorylation at Ser232, Ser293 and Ser300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, at Ser232, Ser293 and Ser300, is required for reactivation. Protein has multiple acetylation sites and acetylation is known to alter the phosphorylation pattern. Dysregulation of PDHE1-A has been implicated in several diseases, including cancer, where its phosphorylation at serine 293 (Ser293) by kinases like ERK2 has been shown to modulate its activity and localization, thereby affecting tumor metabolism and immune evasion. Notably, low phosphorylation levels of PDHE1-A have been correlated with poor prognosis in lung cancer patients, suggesting its potential as a therapeutic target. (Ref.: Zhang, Y., et al.(2022). Nat Metab, 4(3); 374-388; Deng, L., et al. (2022). Front Pharmacol. 13;947372).

~43 kDa observed

Epitope: Phosphorylated Ser293

KLH-conjugated linear peptide corresponding to 11 amino acids surrounding phosphoserine 293 from the C-terminal half of human PDHE1-A type I.

Affinity purified

Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.