Phospho-Pyruvate Dehydrogenase α1 (Ser293) (E4V9L) Rabbit mAb #37115
- WB
- IP
- IF
- F
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 43 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:400 - 1:1600 |
| Flow Cytometry (Fixed/Permeabilized) | 1:400 - 1:1600 |
Storage
For a carrier free (BSA and azide free) version of this product see product #48447.
Protocol
Specificity / Sensitivity
Phospho-Pyruvate Dehydrogenase α1 (Ser293) (E4V9L) Rabbit mAb recognizes endogenous levels of pyruvate dehydrogenase α1 protein only when phosphorylated at Ser293. Based on amino acid sequence comparisons, this antibody is predicted to detect endogenous levels of pyruvate dehydrogenase α2 protein only when phosphorylated at Ser291 residue.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser293 of human pyruvate dehydrogenase α1 protein.
Background
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. The reaction of oxidative decarboxylation of pyruvate serves as a critical link between glycolysis and the citric acid cycle. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is composed of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration, and early death (2).
Pyruvate dehydrogenase kinase 1 phosphorylates pyruvate dehydrogenase (E1) α1 subunit at Ser293 to inactivate its activity (3,4). This phosphorylation contributes to the tumor metabolic reprogramming toward glycolysis in hypoxia by inhibiting the citric acid cycle (4).
Limited Uses
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