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ABS194

Sigma-Aldrich

Anti-phospho PDHE1-A type I (Ser300) Antibody

from rabbit, purified by affinity chromatography

Synonyme(s) :

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial, PDHE1-A type I

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

human

Réactivité de l'espèce (prédite par homologie)

mouse (based on 100% sequence homology), rat (based on 100% sequence homology), bovine (based on 100% sequence homology), Xenopus (based on 100% sequence homology), zebrafish (based on 100% sequence homology)

Technique(s)

immunocytochemistry: suitable
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

phosphorylation (pSer300)

Informations sur le gène

human ... PDHA1(5160)

Description générale

In many organisms, the pyruvate dehydrogenase complex catalyzes the overall, irreversible conversion of pyruvate to acetyl-CoA and CO2 in the aerobic, energy-generating pathways, in addition to serving as a key regulator for cardiac substrate selection. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). PDH is regulated by both pyruvate dehydrogenase kinase (PDK)-mediated phosphorylation and feedback inhibition.

Spécificité

This antibody recognizes PDHE1-A type I phosphorylated at Ser300.

Immunogène

KLH-conjugated linear peptide corresponding to human PDHE1-A type I phosphorylated at Ser300.
Épitope : Phosphorylated Ser300

Application

Analyse par immunocytochimie : A 1:500 dilution from a representative lot detected PDHE1-A type I in dichloroacetate untreated and treated HEK 293 cells.
This Anti-phospho PDHE1-A type I (Ser300) Antibody is validated for use in WB, IC for the detection of phospho PDHE1-A type I (Ser300).

Qualité



µµ

Description de la cible

Poids observé : ~43 kDa

Remarque sur l'analyse


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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Jinxin Liu et al.
Theranostics, 11(17), 8283-8300 (2021-08-11)
Rationale: The molecular mechanisms underlying the pathogenesis of systemic insulin resistance in type 2 diabetes remain elusive. Growth hormone receptor (GHR) deficiency has long been known to improved insulin sensitivity. However, whether hepatic GHR overexpression or activation is a cause
Yuan Z Feng et al.
Journal of lipid research, 58(11), 2147-2161 (2017-08-22)
Lipid droplet (LD) coating proteins are essential for the formation and stability of intracellular LDs. Plin2 is an abundant LD coating protein in skeletal muscle, but its importance for muscle function is unclear. We show that myotubes established from Plin2-/-
Kenichi Aizawa et al.
Cells, 13(1) (2024-01-11)
Heart failure with reduced ejection fraction (HFrEF) is characterized not only by reduced left ventricular ejection fraction (EF) but is also combined with symptoms such as dyspnea, fatigue, and edema. Several pharmacological interventions have been established. However, a treatment targeting
Oxana V Denisova et al.
Molecular oncology, 17(9), 1803-1820 (2023-07-17)
Mitochondrial glycolysis and hyperactivity of the phosphatidylinositol 3-kinase-protein kinase B (AKT) pathway are hallmarks of malignant brain tumors. However, kinase inhibitors targeting AKT (AKTi) or the glycolysis master regulator pyruvate dehydrogenase kinase (PDKi) have failed to provide clinical benefits for
Hao Shi et al.
Molecular metabolism, 11, 160-177 (2018-03-12)
Given that cellular O-GlcNAcylation levels are thought to be real-time measures of cellular nutrient status and dysregulated O-GlcNAc signaling is associated with insulin resistance, we evaluated the role of O-GlcNAc transferase (OGT), the enzyme that mediates O-GlcNAcylation, in skeletal muscle.

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